Kandi Burruss is flaunting a gorgeous cleavage in this video that she shared on her social media account. You can also check it out below.
'Today started off right! Thank you, @georgemiguelc & @theglamfather, for getting me all the way together! Of course, I was styled by @therealnoigjeremy,' Kandi said.
RELATED: Kandi Burruss Celebrates Her Half Sister's Birthday - Fans Are Surprised To See Rebekah
One other follower said: '@kandi, I swear you are ageing backwards, Sis😍😍' and someone else said: 'I love the talks being posted between you and Don Juan. You are a true boss and a class act. I love to see it.'
One followewr said: 'Kandi!! Hi, y'all! I wrote a diverse children's book: "Black, Brown or White We All Feel", Available on Amazon. Reinforces positive behaviour in our children. Inspired by my bullied 5-year-old,' and a fan posted this: 'yes kandi, you always been beautiful, but girl you been serving lately.'
Kandi Burruss addressed the RHOA reunion part one, which will take place this week. Check out the post that she shared in her social media account below.
'They said the theme is Burlesque, 50 shades of grey, dungeon vibes. 😜You know I love a theme! Reunion part one is Sunday. Get ready!' Kandi captioned her post.
Kandi Burruss shared some pics in which she's making some really funny faces. Fans cannot have enough of her, and you can also check out her looks below.
'I can not control my faces! These looks at the gift exchange for @cynthiabailey's #FriendsMas are hilarious! 🤪,' Kandi captioned her post.
Princess Diana's genius fashion hack revealed | HELLO!
Princess Diana was one of the most photographed women in the world and she never failed to look incredible, whether she was wearing elegant dresses or casual gym gear.
But on the many occasions that she would don her finest wear for formal events, Diana was rarely seen without a small matching clutch bag in tow – and there was a very good reason for it.
The late princess would use her clutch – which always matched her evening dress – to cover her chest so she didn't reveal more than she wanted when she exited a car.
Diana even coined a clever name for her fashion hack, according to handbag designer Anya Hindmarsh, who previously told The Telegraph : " We used to laugh when we designed what she called her 'cleavage bags', little satin clutches which she would cover her cleavage with when she stepped out of cars."
"She was a very loyal customer and a lot of fun," Anya added. "She would come and see us with no bodyguards or any fuss."
MORE: Prince William and Prince Harry agree on beautiful tribute for late mother Princess Diana
The Duchess of Cambridge is often spotted holding her bag in her left hand so that she can keep her right hand free to greet and shake hands with guests.
The Queen also reportedly uses her famous Launer purse to send secret messages to her staff. When Her Majesty switches her bag from one arm to the other, it's said to be her way of silently indicating that she'd like to wrap up her current conversation.
How SARS-CoV-2 first adapted in humans | Science
Viruses need entry proteins to penetrate the cells where they will replicate. The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) version is called the spike or S protein. The S protein, also the target of the current vaccines, is quickly adapting to its new human hosts. It took its first major step in this direction early in 2020, when its amino acid 614 (of 1297) changed from an aspartic acid (D) to a glycine (G). Viruses bearing this D614G mutation transmit among humans more rapidly and now form the majority in circulation. On page 525 of this issue, Zhang et al. ( 1 ) use careful structural analyses to reveal how D614G changed the S protein to accelerate the pandemic.
This fix solved a technical problem, but it deepened a mystery. Although a number of distantly related coronaviruses carry furin cleavage sites at their S1-S2 boundaries, the SARS-CoV-1 S protein, and those of all known bat-derived viruses from the same Sarbecovirus lineage, lack this site. Instead of being cleaved in virus-producing cells, their S proteins are cleaved by different proteases while the virus is engaging ACE2 in the next, yet-to-be-infected cell ( 5 ). As it happened, furin-site mutations that improved SARS-CoV-2 S-protein function in pseudoviruses allowed the modified S protein to work with these later-stage enzymes, just like the SARS-CoV-1 version. Why then did the SARS-CoV-2 furin site persist, even though it made infection in cell culture less efficient? Indeed, viruses passaged in culture regularly lost this site. Does it somehow improve viral transmission? Would it eventually disappear over the course of the pandemic?
The underlying mechanism for this fitness advantage remained a point of controversy. Here, a second unusual property of the S protein, in this case shared with SARS-CoV-1, became relevant. The SARS-CoV-2 S protein, like most entry proteins of viruses with a lipid membrane, assembles into trimers. Typically, during the process of virion assembly, viral entry proteins subtly change their conformations, but it is unusual for these proteins to break their three-fold symmetry before they bind their receptor. However, the mature SARS-CoV-2 S protein often assumes an asymmetrical arrangement whereby one of its three RBDs assumes an open or "up" conformation ( 1 , 9 ). Only RBDs in this up conformation can bind ACE2. Once it does so, the S1 domains dissociate from S2, and S2 undergoes a pronounced rearrangement to a "postfusion" state. The released energy of this rearrangement drives the viral and cell membranes to fuse and gives the virus access to the cell interior.
The Gly 614 (G614) mutation in spike (S) increases ordering of the 630 loop compared with wild-type Asp 614 (D614). This prevents the premature S1 shedding often seen with wild-type S proteins, ensuring that more S protein remains in a fusion-ready "one-up" state, with one receptor binding domain (RBD) exposed within the trimer, ready to bind angiotensin-converting enzyme 2 (ACE2) on host cells, increasing infection efficiency.
To cut through this controversy, Zhang et al. solved the structure and provided detailed analyses of both D614 and G614 S proteins in multiple states. They first noted that, as they and others had previously observed, the loss of D614 in S1 breaks an ionic bond to a proximal lysine, K854, in S2 ( 9 ). Loss of this salt bridge is initially counterintuitive because it would loosen the association between S1 and S2, although it might ease the movement of the RBD into the up configuration. However, the structures from Zhang et al. show that a major difference between S proteins with and without D614G is the visibly greater ordering in G614 S proteins of a region spanning residues 620 to 640, which the authors call the "630 loop." This loop is just downstream of G614. It is therefore possible that either the loss of the D614-K854 salt bridge, or the greater backbone flexibility that a glycine affords, helps the 630 loop nestle more tightly in a canyon formed by two larger S-protein domains (the amino-terminal domain and carboxyl-terminal domain 1). Regardless, this loop is found in a more rigid and stable arrangement between these domains when residue 614 is a G than when it is a D.
The key is that both the RBD-up conformation and dissociation of S1 from S2—enabled by furin cleavage—require disordering of the 630 loop. Thus, the RBD-up conformation can be more easily accessed with the original D614 S protein, but once this conformation is achieved, this S protein is more likely to fall apart entirely owing to premature shedding of its S1 domain. Conversely, with G614, more energy is required to achieve a one RBD–up state, but dissociation of S1 from S2 also becomes less favorable because the remaining folded 630 loops continue to hold the trimer together. Thus, the D614G variants have more S proteins in the up orientation because the next, irreversible step toward inactivation is slower. Infection with D614G is more efficient because it prevents premature S1 shedding (see the figure).
Structural impact on SARS-CoV-2 spike protein by D614G substitution | Science
Throughout the COVID-19 pandemic, epidemiologists have monitored the evolution of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) with particular focus on the spike protein. An early variant with an aspartic acid (D) to glycine (G) mutation at position 614, D614G, rapidly became dominant and is maintained in current variants of concern. Zhang et al. investigated the structural basis for the increased spread of this variant, which does so even though it binds less tightly to the host receptor (see the Perspective by Choe and Farzan). Structural and biochemical studies on a full-length G614 spike trimer showed that there are interactions not present in D614 that prevent premature loss of the S1 subunit that binds angiotensin-converting enzyme 2. This stabilization effectively increases the number of spikes that can facilitate infection.
Substitution for aspartic acid (D) by glycine (G) at position 614 in the spike (S) protein of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) appears to facilitate rapid viral spread. The G614 strain and its recent variants are now the dominant circulating forms. Here, we report cryo–electron microscopy structures of a full-length G614 S trimer, which adopts three distinct prefusion conformations that differ primarily by the position of one receptor-binding domain. A loop disordered in the D614 S trimer wedges between domains within a protomer in the G614 spike. This added interaction appears to prevent premature dissociation of the G614 trimer—effectively increasing the number of functional spikes and enhancing infectivity—and to modulate structural rearrangements for membrane fusion. These findings extend our understanding of viral entry and suggest an improved immunogen for vaccine development.
( A ) The full-length SARS-CoV-2 S protein carrying either D614 or G614 was extracted and purified in detergent n-dodecyl-β- d -maltopyranoside (DDM) and further resolved by gel-filtration chromatography on a Superose 6 column. The molecular weight standards include thyoglobulin (670 kDa), γ-globulin (158 kDa), and ovalbumin (44 kDa). Peak I is the prefusion S trimer; peak II is the postfusion S2 trimer, and peak III is the dissociated monomeric S1. The insets show peak fractions that were analyzed by Coomassie-stained SDS-PAGE. Labeled bands are S, S1, and S2. Fr#, fraction number. ( B ) Binding analysis of fractions of peak I in (A) with soluble ACE2 constructs by BLI. The purified S proteins were immobilized to AR2G biosensors and dipped into the wells containing ACE2 at various concentrations (5.56 to 450 nM for monomeric ACE2; 2.78 to 225 nM for dimeric ACE2). Binding kinetics was evaluated using a 1:1 Langmuir binding model for the monomeric ACE2 and a bivalent model for dimeric ACE2. The sensorgrams are in black and the fits in red. Binding constants are also summarized here and in table S1. All experiments were repeated at least twice with essentially identical results. K D , dissociation constant (binding affinity); RU, response unit.
( A ) Three structures of the G614 S trimer—representing a closed, three RBD–down conformation; an RBD-intermediate conformation; and a one RBD–up conformation—were modeled on the basis of corresponding cryo-EM density maps at 3.1- to 3.5-Å resolution. Three protomers (a, b, and c) are colored in red, blue, and green, respectively. RBD locations are indicated. ( B ) Top views of the superposition of the three structures of the G614 S in (A) in ribbon representation, with the structure of the prefusion trimer of the D614 S (Protein Data Bank ID: 6XR8) shown in yellow. The NTD and RBD of each protomer are indicated. Side views of the superposition are shown in fig. S8.
To examine the structural changes resulting from the D614G substitution, we superposed the structures of the G614 trimer onto the D614 trimer in the closed conformation, aligning them by the invariant S2 ( Fig. 2B ). A shift by a clockwise, outward rotation of all three S1 subunits, relative to the D614 structure, is evident even for the G614 trimer in the closed conformation. A similar shift was also observed in the RBD-intermediate and RBD-up G614 structures. Thus, the D614G substitution has led to a slightly more open conformation than that of the D614 trimer, even when all three RBDs are down. The D614G change has apparently also rigidified a neighboring segment of CTD2, residues 620 to 640, which we designate the 630 loop. This loop inserts into a gap, slightly wider in the G614 than in the D614 trimer, between the NTD and CTD1 of the same protomer ( Figs. 3 and 4 ). The 630 loop is disordered in the closed D614 trimer (fig. S10) because the gap is too narrow for it to insert. The closed D614 trimer thus has three ordered FPPRs and three disordered 630 loops, whereas the closed G614 trimer has three structured 630 loops along with three ordered FPPRs. In the two conformers with one partly or fully open RBD, the two segments are disordered in the RBD-shifted subunit, and their central parts have difficult-to-model densities in one other subunit. The third pair appears well ordered throughout ( Fig. 3 ). Thus, the opening of the RBD in the full-length G614 trimer correlates with a displacement of the 630 loop and the FPPR having moved away from its position in the D614 trimer.
( A ) (Top) The structure of the closed, three RBD–down conformation of the D614 S trimer is shown in ribbon diagram with one protomer colored as NTD in blue, RBD in cyan, CTD1 in green, CTD2 in light green, S2 in light blue, the 630 loop in red, and the FPPR in magenta. (Bottom) Structures of three segments (residues 617 to 644) containing the 630 loop in red and three segments (residues 823 to 862) containing the FPPR in magenta from all three protomers (a, b, and c) are shown. The position of each RBD is indicated. ( B to D ) Structures of the G614 trimer in the closed, three RBD–down conformation, the RBD-intermediate conformation, and the one RBD–up conformation, respectively, are shown, as in (A). Dashed lines indicate gaps.
( A ) A close-up view of the region near the residue 614 with superposition of the G614 trimer structure in green (CTD2) and magenta (FPPR) and the D614 trimer in yellow, both in the closed prefusion conformation. Residues G614, D614, and two K854s from both structures are shown in stick model. The direction of the three-fold axis of the trimer is indicated. ( B ) Location of the 630 loop in the S trimer. The 630 loop is highlighted in red, the NTD in blue, the CTD1 in green, the CTD2 in light green, the S2 in light blue, and the FPPR from a neighboring protomer in magenta. The S1-S2 boundary and the nearest ordered residues Thr 676 from S1 and Ser 689 from S2 are all indicated. A strand from the N-terminal end of S2, packed in the CTD2, is highlighted in purple. ( C ) A view showing that the 630 loop wedges between the NTD and the CTD1 and pushes them apart. ( D ) Packing of the 630 loop against the hydrophobic surface formed by residues Val 595 , Val 597 , Val 610 , Tyr 612 , Val 642 , and Ile 651 from the CTD2 and Pro 295 from the NTD. Residues Trp 633 and Val 635 from the 630 loop contribute to this interaction.
CTD2 is formed by two stacked, four-stranded β sheets, with a fifth strand in one sheet contributed by the connector between the NTD and RBD. In the other sheet, an interstrand loop contains the S1-S2 cleavage site, and thus one strand is the N-terminal segment of S2 ( Fig. 4B ). In the G614 trimer, one side of the 630 loop packs along a long hydrophobic surface, largely solvent-exposed in the D614 trimer, formed by residues on the upward-facing surface of the CTD2 along with Pro 295 from the NTD ( Fig. 4D ). Trp 633 and Tyr 636 of the 630 loop appear to contribute to this interaction. S1 dissociation from S2 requires breaking the S2 strand from the second β sheet. An ordered 630 loop that stabilizes the CTD2 by closing off an exposed, hydrophobic surface may retard S1 shedding, thereby enhancing the stability of a cleaved S trimer. We note that the density for a fatty acid ligand making contacts with the neighboring RBDs in the D614 trimer is absent in all of the G614 reconstructions (fig. S11C) ( 37 ), which suggests that the ligand is not required for three RBDs to adopt the down conformation.
To test the impact of the 630 loop on S1 shedding and membrane fusion, we generated five S mutants, each containing a single-residue change either in the 630 loop (W633A, R634E, V635K, and Y636A) or the CTD2 hydrophobic surface (V610K) in the G614 sequence. These mutants expressed the same levels of S, with similar extents of cleavage between S1 and S2, as expected (fig. S12A). When detected by monoclonal antibodies using flow cytometry, mutants V610K and W633A showed markedly lower binding of RBD-specific antibodies [REGN10933 and REGN10987; ( 38 )] and of an NTD-specific antibody [4A8; ( 39 )] than the parental G614 S, whereas binding to an S2-specific antibody [0304-3H3; ( 39 )] was slightly higher (fig. S12B). These results are consistent with the hydrophobic interactions between the 630 loop and CTD2 stabilizing the cleaved S1-S2 complex and preventing S1 dissociation. The mutant V635K had wild-type phenotypes in these assays, likely because V635 does not make any direct contact with the CTD2. The mutants R634E and Y636A showed intermediate levels of antibody binding because Y636 appears to contribute less to the 630 loop–CTD2 interaction than W633, and R634 may help maintain the loop's overall shape for inserting between domains. Likewise, a similar pattern was observed with these mutants in the cell-cell fusion assay, except that Y636A showed substantially weaker fusion activity than R634E (fig. S12C). Thus, key residues important for stabilizing the S trimer structure appear critical for membrane fusion activity, as premature dissociation of S1 would lead to inactivation of the S trimer.
Digital PCR Detection of mtDNA/gDNA Ratio in Embryo Culture Medium for | PGPM
Digital PCR Detection of mtDNA/gDNA Ratio in Embryo Culture Medium for Prediction of Embryo Development Potential
Noninvasive embryo screening technology is a new method to evaluate the contents of metabolites and nutrients in embryo culture medium. During the development of embryo, the contents of mitochondrion in the blastomere decreased gradually, and the contents of cell-free mtDNA in the corresponding embryo medium increased. It has been studied that the ratio of mtDNA/gDNA in embryo culture medium can be used to predict embryo development, but its predictive value is controversial, while the positive detection rate of gDNA is low, and a more accurate technology is to be found for verification. In this study, we used digital PCR system to explore the relationship between cell-free mtDNA in culture medium and the development potential of embryo. The mtDNA/gDNA ratio is associated with the cleavage stage embryo rating, fragmentation, and developmental state, and correlates with the blastocyst rating. According to our research, shortcomings are still associated with using only this indicator to predict embryonic development potential.
New techniques to screen for the highest quality embryos for transfer can reduce transfer embryo numbers, improve pregnancy outcomes, and reduce the risk of multiple births. This topic has become a focus of assisted reproductive technology (ART) research. Selective single blastocyst transplantation can improve pregnancy rates and reduce the risk of multiple pregnancies. 1 Embryos during the cleavage and blastocyst phases have been rated during in vitro fertilization (IVF) using morphological scoring methods. Some of these screening metrics have been applied to predict developmental potential including embryonic development speed, degrees of uneven blastomere cleavage, fragment content, inner cell mass (ICM), and trophectoderm (TE) levels. 2–6 However, that the best quality embryos will be selected for transfer is not guaranteed. Because morphology can appear normal, morphological screening cannot detect genetic defects, nor can it completely ensure optimal embryo development potential. Traditional observation at a fixed time point will miss some important parameters and key events during embryonic development. These parameters are all related to embryonic development potential, and to achieve standardization by relying on subjective differences in artificial observation scores is difficult. 7–9
After ICSI fertilization, embryos were cultured to the blastula stage in Sydney IVF Cleavage Medium (Cook Medical Inc., Bloomington, IN, USA) then transferred to blastocyst culture medium for embryo exchange on day 3. The cultures were placed in MINC ® Benchtop Incubators (Cook Medical Inc.) and only 2PN-derived embryos were collected. We sampled 20 μL of CM culture media per embryo in DNase and RNase-free sterile PCR tubes and froze them at −40°C. Unused culture medium was the negative control.
Free DNA in culture medium was purified using QIAamp Circulating Nucleic Acid kit (Qiagen, Hilden, Germany) as described by the manufacturer, mixed with 30 μL of elution buffer, then quantified using a NanoDrop 2000 spectrophotometer (Thermo Scientific Inc., Waltham, MA, USA).
We established a digital PCR detection system with reference to primers in the literature. We then optimized and amplified the D-loop region of the mitochondrial (NC_012920.1) gene, and β-actin (NG_007992.1) was the internal reference gene. Table 1 shows the primers and probes.
Table 1 Primer and Probe Sequences
We used a QX200 droplet dPCR system (Bio-Rad Laboratories Inc., Hercules, CA, USA). We found mtDNA in 223 samples, (Average: 219.80, n = 223). We did not detect gDNA in 25 samples (Average: 8.04, n = 198), and the minimum detection value was 1.8. Therefore, the number of copies of gDNA that were not detected were counted as 1.8.
The primers and probes in this paper were diluted to 10μM (10μmol/L). Reaction mixtures (20 μL) contained 10 μL ddPCR Supermix for Probes (No dUTP) (Bio-Rad Laboratories Inc.), forward and reverse primers (1.8 µL) for the target and β-actin genes, the target gene probe (0.4 µL), the β-actin gene probe (0.4 µL), and 2 µL of template.
Reaction mixtures (20 µL) were added to 8 holes in the middle row of a DG8 cartridge (20 μL X control buffer doubled for ~8 samples). About 70 µL of microdrop-generated (DG) oil was added to the bottom row of 8 holes in the cartridges, and all holes were filled. The gasket was covered and all holes on both sides were secured. The holder was placed above the QX200 microdroplet generator to produce microdroplets for 2 minutes in the top row of the cartridge. These were then transferred to 96-well plates, covered with a membrane and heat-sealed.
Nature Journal: Reflections on glittering 'mica' minerals
Two thousand years BC, when thin sheets were used as surfaces for painting mythological scenes, it was supposed that mica represented the preserved form of lightning flashes.
It is a generic term that applies to a group of complex minerals with a sheet or plate-like structure. All micas form flat six-sided crystals with cleavage parallel to the direction of the large surfaces, which permits them to be split into optically flat films.
Muscovite micas, which are colorless to pale green in color, are more easily split than others. The designation "muscovite" was derived from Muscovia, the district in Russia where the mineral was found and identified in the early seventeenth century. "Sheet" mica refers to books (or lenses) mined from either hard rock or loosely consolidated clayey materials. These can be readily split into specific thicknesses.
The Peabody Museum at Harvard has a beautiful serpent carved from trade mica. The surface is scored with shallow decorative incision marks in the location of the serpent's head. These perhaps signify the horned serpent figure similar to the Uktenas in Cherokee lore. The cut-out was assembled from a total of twelve mica fragments.
In other words, the Native Americans were meticulous when it came to crafting mica ornamentals. It was the material of choice for artwork throughout eastern North America for centuries — and the Cherokees had prospecting rights. .
Before mica mining became a multimillion dollar industrial enterprise in the area of Spruce Pine north of Asheville, it was a cottage industry. In The French Broad (1965), one of my favorite books, Wilma Dykeman, one of my favorite people, described those days:
"A large part of this mining is done in small operations — `groundhog holes,' the local people call them, penetrating the sides of hill after hill in these counties (Mitchell, Yancey and parts of Avery), and the raw wound of many an abandoned digging gapes on the mountainside, giving the country an appearance different from the rest of the French Broad watershed."
She also noted that it was during the post-Civil War era — "when a northern traveler happened to see a large sheet of `isinglass' in one of the cabins, where he stopped overnight" — that the sheet-mica business was initiated, thereby supplying "practically all of the isinglass used in the old-fashioned stove windows in this country or Canada." Big sheets of mica used for cabin or store windows were called isinglass. Smaller pieces were also crafted into kerosene lamp chimneys.
The center of mica production has traditionally been in the Spruce Pine area, but there were also extensive mines in Jackson and Macon counties. In "The History of Jackson Country" (1987), John L. Bell notes that mica deposits were first discovered "on the road between Webster and Franklin" in 1858. These were displayed at the South Carolina State Fair in 1866. As recently as the early 1940s, "the defense needs of World War II caused a boom in mica," then very "important in the production of electronic vacuum tubes. Ninety-four mines were opened in 1942, but "only 30 were operating in 1943 because of the manpower shortage."
Rosie Huntington-Whiteley turns heads in an aquamarine mini dress on date night with Jason
And Rosie Huntington-Whiteley, 34, ensured all eyes would be on her as she enjoyed a date night with fiancé Jason Statham, 53, at Nobu in Malibu on Wednesday.
Strutting into the venue in an eye-catching blue twinset, the Vogue cover girl was a vision of beauty on the outing.
Rosie opted for an aquamarine midi dress with a scooped neckline that showcased her cleavage and a cut out hem that put her tanned and toned pins on full display.
She teamed the garment with a cardigan in the same striking blue that complemented her golden complexion.
Boosting her 5′ 9″ model frame, the mother-of-one teetered along in a pair of peach barely-there heels and tucked a knitted white clutch bag under her arm.
Jason looked typically dapper as he donned a navy suit over a white T-shirt teamed with smart trainers.
The pair were enjoying some quality couple time as their three-year-old son Jack, did not join them for dinner.
Rebecca Lobie flaunts her assets in a pink latex dress amid OnlyFans rumours | Daily Mail Online
She's rumoured to be starting her own OnlyFans account soon, after gaining more than 100,000 followers on Instagram thanks to her raunchy photos.
And Rebecca Lobie did little to quell the speculation on Thursday as she flaunted her sensational figure in a skintight latex dress in her latest upload.
The 'hot niece' of late wildlife conservationist Steve Irwin showcased her ample cleavage and toned legs in the flirty pink number.
'My fav party dress': Steve Irwin's 'hot niece' Rebecca Lobie flaunted her sensational figure in a skintight latex dress on Thursday amid rumours she's starting an OnlyFans account
She styled her blonde hair straight, opted for a glamorous makeup palette, and boosted her height with a pair of perspex heels.
'My fav party dress. Can't wait to head to the goldy again soon!' wrote the Sunshine Coast-based mother of two, 33, referring to her upcoming trip to the Gold Coast.
Rebecca shared another snap on her Instagram Stories of herself modelling a personalised sleepwear set, with her name 'Bec' printed on the front.
Over the weekend, Rebecca left fans wondering whether she's set to monetise her racy photos by starting an OnlyFans account.
Paris Hilton wows in a semi-sheer white dress with puffy sleeves | Daily Mail Online
And Paris Hilton was sure to turn heads in a clip she shared via Instagram stories on Wednesday that saw her dance at home to Diana Ross and The Supremes.
The socialite, 40, looked sensational as she slipped into a semi-sheer white dress that had dramatic puffy sleeves.
Wow! Paris Hilton looked sensational as she slipped into a semi-sheer white dress with puffy sleeves while dancing at home in a stylish clip she shared via Instagram on Wednesday
Paris' ensemble had a low-cut scooped neckline and was semi-sheer to show off a glimpse of her cleavage while she twirled around a room in her house.
The outfit also had a tulle skirt that fell to the floor and which the reality star pulled up around and over her face.
Her golden locks were brushed into a sleek, straight style and she wore a light palette of make-up for the occasion.
Paris also made sure that all attention remained on her ensemble by keeping her accessories to a minimum and just wearing diamond stud earrings.
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