Cell Surface最新文献

{"title":"Fluconazole resistant Candida auris clinical isolates have increased levels of cell wall chitin and increased susceptibility to a glucosamine-6-phosphate synthase inhibitor","authors":"Garima Shahi ,&nbsp;Mohit Kumar ,&nbsp;Andrzej S. Skwarecki ,&nbsp;Matt Edmondson ,&nbsp;Atanu Banerjee ,&nbsp;Jane Usher ,&nbsp;Neil A.R. Gow ,&nbsp;Sławomir Milewski ,&nbsp;Rajendra Prasad","doi":"10.1016/j.tcsw.2022.100076","DOIUrl":"10.1016/j.tcsw.2022.100076","url":null,"abstract":"<div><p>In 2009 <em>Candida auris</em> was first isolated as fungal pathogen of human disease from ear canal of a patient in Japan. In less than a decade, this pathogen has rapidly spread around the world and has now become a major health challenge that is of particular concern because many strains are resistant to multiple class of antifungal drugs. The lack of available antifungals and rapid increase of this fungal pathogen provides an incentive for the development of new and more potent anticandidal drugs and drug combinatorial treatments. Here we have explored the growth inhibitory activity against <em>C. auris</em> of a synthetic dipeptide glutamine analogue<strong>,</strong> L-norvalyl-<em>N</em>³-(4-methoxyfumaroyl)-L-2,3- diaminopropanoic acid (Nva-FMDP), that acts as an inhibitor of glucosamine-6-phosphate (GlcN-6-P) synthase - a key enzyme in the synthesis of cell wall chitin. We observed that in contrast to FLC susceptible isolates of <em>C. auris</em>, FLC resistant isolates had elevated cell wall chitin and were susceptible to inhibition by Nva-FMDP. The growth kinetics of <em>C. auris</em> in RPMI-1640 medium revealed that the growth of FLC resistant isolates were 50–60% more inhibited by Nva-FMDP (8 <span><math><mi>μ</mi></math></span> g/ml) compared to a FLC susceptible isolate. Fluconazole resistant strains displayed increased transcription of <em>CHS1, CHS2</em> and <em>CHS3,</em> and the chitin content of the fluconazole resistant strains was reduced following the Nva-FMDP treatment<em>.</em> Therefore, the higher chitin content in FLC resistant <em>C. auris</em> isolates may make the strain more susceptible to inhibition of the antifungal activity of the Nva-FMDP peptide conjugate.</p></div>","PeriodicalId":36539,"journal":{"name":"Cell Surface","volume":"8 ","pages":"Article 100076"},"PeriodicalIF":0.0,"publicationDate":"2022-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2468233022000056/pdfft?md5=116e15e3913ed13bad2a3c8d00e6b500&pid=1-s2.0-S2468233022000056-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"42833030","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Discovery, mode of action and secretion of Burkholderia sensu lato key antimicrobial specialised metabolites","authors":"Yoana D. Petrova ,&nbsp;Eshwar Mahenthiralingam","doi":"10.1016/j.tcsw.2022.100081","DOIUrl":"10.1016/j.tcsw.2022.100081","url":null,"abstract":"<div><p><em>Burkholderia</em> sensu lato bacteria have genomes rich in biosynthetic gene clusters (BGCs) encoding for multiple bioactive specialised metabolites. Diverse classes of antimicrobial natural products have been isolated from <em>Burkholderia</em>, including polyynes, shikimate pathway derivatives, polyketides, non-ribosomal peptides and hybrid polyketide non-ribosomal peptides. We highlight examples of <em>Burkholderia</em> metabolites, overviewing their biosynthesis, bioactivity, mechanisms of action and secretion.</p></div>","PeriodicalId":36539,"journal":{"name":"Cell Surface","volume":"8 ","pages":"Article 100081"},"PeriodicalIF":0.0,"publicationDate":"2022-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9579380/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40676554","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The nature of the fungal cargo induces significantly different temporal programmes of macrophage phagocytosis","authors":"María Fernanda Alonso ,&nbsp;Judith M. Bain ,&nbsp;Fiona M. Rudkin ,&nbsp;Lars P. Erwig ,&nbsp;Alistair J.P. Brown ,&nbsp;Neil A.R. Gow","doi":"10.1016/j.tcsw.2022.100082","DOIUrl":"10.1016/j.tcsw.2022.100082","url":null,"abstract":"<div><p>Phagocytosis is an essential component of our immune defence against fungal pathogens. Differences in the dynamics of phagocyte migration, recognition, uptake and phagolysosome maturation are dependent on the characteristics of the fungal cargo, and in particular to differences in cell wall composition and cellular morphology. However, studies that have focused on phagocyte interactions with individual fungal species have not enabled comparisons in the kinetics of these interactions to be made between these different species. We therefore used live cell video microscopy to examine the temporal dynamics of phagocytosis for a range of fungal cargoes by thioglycollate–elicited peritoneal macrophages from C57BL/6 mice. Uniform populations of macrophages were challenged at the same time with yeast cells of <em>Candida albicans</em>, <em>Candida glabrata, Saccharomyces cerevisiae</em> and <em>Cryptococcus neoformans</em> (wild–type and an acapsular mutant, <em>cap</em>59Δ), and spores of <em>Aspergillus fumigatus</em> and <em>Mucor circinelloides</em> to enable standardized comparative interactions to be quantified from different stages of phagocytosis<em>.</em> Differences in the rate of uptake of fungal cells varied by up to 26–fold, whilst differences in time to induce phagosome acidification varied by as much as 29–fold. Heat-killing or opsonizing the fungal targets markedly affected the kinetics of the interaction in a species–specific manner. Fungal and macrophage killing assays further revealed cargo–specific differences in phagocytosis and diversity in fungal evasion mechanisms. Therefore, simultaneous assessment of the interaction of macrophages with different fungal pathogens highlighted major differences in the kinetics and growth responses during fungus–phagocyte interactions that are likely to impact on pathogenesis and virulence.</p></div>","PeriodicalId":36539,"journal":{"name":"Cell Surface","volume":"8 ","pages":"Article 100082"},"PeriodicalIF":0.0,"publicationDate":"2022-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9589029/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9722796","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"A review on pilus assembly mechanisms in Gram-positive and Gram-negative bacteria","authors":"Tamilarasi Shanmugasundarasamy,&nbsp;Deenadayalan Karaiyagowder Govindarajan,&nbsp;Kumaravel Kandaswamy","doi":"10.1016/j.tcsw.2022.100077","DOIUrl":"10.1016/j.tcsw.2022.100077","url":null,"abstract":"<div><p>The surface of Gram-positive and Gram-negative bacteria contains long hair-like proteinaceous protrusion known as pili or fimbriae. Historically, pilin proteins were considered to play a major role in the transfer of genetic material during bacterial conjugation. Recent findings however elucidate their importance in virulence, biofilm formation, phage transduction, and motility. Therefore, it is crucial to gain mechanistic insights on the subcellular assembly of pili and the localization patterns of their subunit proteins (major and minor pilins) that aid the macromolecular pilus assembly at the bacterial surface. In this article, we review the current knowledge of pilus assembly mechanisms in a wide range of Gram-positive and Gram-negative bacteria, including subcellular localization patterns of a few pilin subunit proteins and their role in virulence and pathogenesis.</p></div>","PeriodicalId":36539,"journal":{"name":"Cell Surface","volume":"8 ","pages":"Article 100077"},"PeriodicalIF":0.0,"publicationDate":"2022-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2468233022000068/pdfft?md5=462727c0a092901e1369f5b31494b1b7&pid=1-s2.0-S2468233022000068-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"45916442","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Imbalance of peptidoglycan biosynthesis alters the cell surface charge of Listeria monocytogenes","authors":"Lisa Maria Schulz ,&nbsp;Patricia Rothe ,&nbsp;Sven Halbedel ,&nbsp;Angelika Gründling ,&nbsp;Jeanine Rismondo","doi":"10.1016/j.tcsw.2022.100085","DOIUrl":"10.1016/j.tcsw.2022.100085","url":null,"abstract":"<div><p>The bacterial cell wall is composed of a thick layer of peptidoglycan and cell wall polymers, which are either embedded in the membrane or linked to the peptidoglycan backbone and referred to as lipoteichoic acid (LTA) and wall teichoic acid (WTA), respectively. Modifications of the peptidoglycan or WTA backbone can alter the susceptibility of the bacterial cell towards cationic antimicrobials and lysozyme. The human pathogen <em>Listeria monocytogenes</em> is intrinsically resistant towards lysozyme, mainly due to deacetylation and <em>O</em>-acetylation of the peptidoglycan backbone via PgdA and OatA. Recent studies identified additional factors, which contribute to the lysozyme resistance of this pathogen. One of these is the predicted ABC transporter, EslABC. An <em>eslB</em> mutant is hyper-sensitive towards lysozyme, likely due to the production of thinner and less <em>O</em>-acetylated peptidoglycan. Using a suppressor screen, we show here that suppression of <em>eslB</em> phenotypes could be achieved by enhancing peptidoglycan biosynthesis, reducing peptidoglycan hydrolysis or alterations in WTA biosynthesis and modification. The lack of EslB also leads to a higher negative surface charge, which likely stimulates the activity of peptidoglycan hydrolases and lysozyme. Based on our results, we hypothesize that the portion of cell surface exposed WTA is increased in the <em>eslB</em> mutant due to the thinner peptidoglycan layer and that latter one could be caused by an impairment in UDP-<em>N</em>-acetylglucosamine (UDP-Glc<em>N</em>Ac) production or distribution.</p></div>","PeriodicalId":36539,"journal":{"name":"Cell Surface","volume":"8 ","pages":"Article 100085"},"PeriodicalIF":0.0,"publicationDate":"2022-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/45/73/main.PMC9593813.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"10722462","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Plant lectins: Handymen at the cell surface","authors":"Tibo De Coninck,&nbsp;Els J.M. Van Damme","doi":"10.1016/j.tcsw.2022.100091","DOIUrl":"10.1016/j.tcsw.2022.100091","url":null,"abstract":"<div><p>Lectins are carbohydrate-binding proteins and are involved in a multitude of biological functions. Lectins at the surface of plant cells often occur as lectin receptor-like kinases (LecRLK) anchored to the plasma membrane. These LecRLKs are part of the plant’s pattern-recognition receptor (PRR) system enabling the plant to perceive threats and respond adequately. Furthermore, plant lectins also occur as secreted proteins, which are associated with stress signalling and defence. The aim of this short review is to provide a general perspective on plant lectins and their role at the cell surface.</p></div>","PeriodicalId":36539,"journal":{"name":"Cell Surface","volume":"8 ","pages":"Article 100091"},"PeriodicalIF":0.0,"publicationDate":"2022-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/43/2a/main.PMC9713479.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"35345913","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Surfactant protein D inhibits growth, alters cell surface polysaccharide exposure and immune activation potential of Aspergillus fumigatus","authors":"Sarah Sze Wah Wong ,&nbsp;Sarah Dellière ,&nbsp;Natalia Schiefermeier-Mach ,&nbsp;Lukas Lechner ,&nbsp;Susanne Perkhofer ,&nbsp;Perrine Bomme ,&nbsp;Thierry Fontaine ,&nbsp;Anders G. Schlosser ,&nbsp;Grith L. Sorensen ,&nbsp;Taruna Madan ,&nbsp;Uday Kishore ,&nbsp;Vishukumar Aimanianda","doi":"10.1016/j.tcsw.2022.100072","DOIUrl":"10.1016/j.tcsw.2022.100072","url":null,"abstract":"<div><p>Humoral immunity plays a defensive role against invading microbes. However, it has been largely overlooked with respect to <em>Aspergillus fumigatus</em>, an airborne fungal pathogen. Previously, we have demonstrated that surfactant protein D (SP-D), a major humoral component in human lung-alveoli, recognizes <em>A. fumigatus</em> conidial surface exposed melanin pigment. Through binding to melanin, SP-D opsonizes conidia, facilitates conidial phagocytosis, and induces the expression of protective pro-inflammatory cytokines in the phagocytic cells. In addition to melanin, SP-D also interacts with galactomannan (GM) and galactosaminogalactan (GAG), the cell wall polysaccharides exposed on germinating conidial surfaces. Therefore, we aimed at unravelling the biological significance of SP-D during the germination process. Here, we demonstrate that SP-D exerts direct fungistatic activity by restricting <em>A. fumigatus</em> hyphal growth. Conidial germination in the presence of SP-D significantly increased the exposure of cell wall polysaccharides chitin, α-1,3-glucan and GAG, and decreased β-1,3-glucan exposure on hyphae, but that of GM was unaltered. Hyphae grown in presence of SP-D showed positive immunolabelling for SP-D. Additionally, SP-D treated hyphae induced lower levels of pro-inflammatory cytokine, but increased IL-10 (anti-inflammatory cytokine) and IL-8 (a chemokine) secretion by human peripheral blood mononuclear cells (PBMCs), compared to control hyphae. Moreover, germ tube surface modifications due to SP-D treatment resulted in an increased hyphal susceptibility to voriconazole, an antifungal drug. It appears that SP-D exerts its anti-<em>A. fumigatus</em> functions via a range of mechanisms including hyphal growth-restriction, hyphal surface modification, masking of hyphal surface polysaccharides and thus altering hyphal immunostimulatory properties.</p></div>","PeriodicalId":36539,"journal":{"name":"Cell Surface","volume":"8 ","pages":"Article 100072"},"PeriodicalIF":0.0,"publicationDate":"2022-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/02/6e/main.PMC8792412.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39750456","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Molecular sensors reveal the mechano-chemical response of Phytophthora infestans walls and membranes to mechanical and chemical stress","authors":"Lucile Michels ,&nbsp;Jochem Bronkhorst ,&nbsp;Michiel Kasteel ,&nbsp;Djanick de Jong ,&nbsp;Bauke Albada ,&nbsp;Tijs Ketelaar ,&nbsp;Francine Govers ,&nbsp;Joris Sprakel","doi":"10.1016/j.tcsw.2021.100071","DOIUrl":"10.1016/j.tcsw.2021.100071","url":null,"abstract":"<div><p><em>Phytophthora infestans</em>, causal agent of late blight in potato and tomato, remains challenging to control. Unravelling its biomechanics of host invasion, and its response to mechanical and chemical stress, could provide new handles to combat this devastating pathogen. Here we introduce two fluorescent molecular sensors, CWP-BDP and NR12S, that reveal the micromechanical response of the cell wall-plasma membrane continuum in <em>P. infestans</em> during invasive growth and upon chemical treatment. When visualized by live-cell imaging, CWP-BDP reports changes in cell wall (CW) porosity while NR12S reports variations in chemical polarity and lipid order in the plasma membrane (PM). During invasive growth, mechanical interactions between the pathogen and a surface reveal clear and localized changes in the structure of the CW. Moreover, the molecular sensors can reveal the effect of chemical treatment to CW and/or PM, thereby revealing the site-of-action of crop protection agents. This mechano-chemical imaging strategy resolves, non-invasively and with high spatio-temporal resolution, how the CW-PM continuum adapts and responds to abiotic stress, and provides information on the dynamics and location of cellular stress responses for which, to date, no other methods are available.</p></div>","PeriodicalId":36539,"journal":{"name":"Cell Surface","volume":"8 ","pages":"Article 100071"},"PeriodicalIF":0.0,"publicationDate":"2022-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8760408/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39844598","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Biochemical characterization of Pectin Methylesterase Inhibitor 3 from Arabidopsis thaliana","authors":"Fan Xu ,&nbsp;Martine Gonneau ,&nbsp;Elvina Faucher ,&nbsp;Olivier Habrylo ,&nbsp;Valérie Lefebvre ,&nbsp;Jean-Marc Domon ,&nbsp;Marjolaine Martin ,&nbsp;Fabien Sénéchal ,&nbsp;Alexis Peaucelle ,&nbsp;Jérôme Pelloux ,&nbsp;Herman Höfte","doi":"10.1016/j.tcsw.2022.100080","DOIUrl":"10.1016/j.tcsw.2022.100080","url":null,"abstract":"<div><p>The de-methylesterification of the pectic polysaccharide homogalacturonan (HG) by pectin methylesterases (PMEs) is a critical step in the control of plant cell expansion and morphogenesis. Plants have large gene families encoding PMEs but also PME inhibitors (PMEIs) with differ in their biochemical properties. The <em>Arabidopsis thaliana PECTIN METHYLESTERASE INHIBITOR 3 (PMEI3)</em> gene is frequently used as a tool to manipulate pectin methylesterase activity in studies assessing its role in the control of morphogenesis. One limitation of these studies is that the exact biochemical activity of this protein has not yet been determined. In this manuscript we produced the protein in <em>Pichia pastoris</em> and characterized its activity <em>in vitro</em>. Like other PMEIs, PMEI3 inhibits PME activity at acidic pH in a variety of cell wall extracts and in purified PME preparations, but does not affect the much stronger PME activity at neutral pH. The protein is remarkable heat stable and shows higher activity against PME3 than against PME2, illustrating how different members of the large PMEI family can differ in their specificities towards PME targets. Finally, growing <em>Arabidopsis thaliana</em> seedlings in the presence of purified PMEI3 caused a dose-dependent inhibition of root growth associated with the overall inhibition of HG de-methylesterification of the root surface. This suggests an essential <em>in vivo</em> role for PME activity at acidic pH in HG de-methylesterification and growth control. These results show that purified recombinant PMEI3 is a powerful tool to study the connection between pectin de-methylesterification and cell expansion.</p></div>","PeriodicalId":36539,"journal":{"name":"Cell Surface","volume":"8 ","pages":"Article 100080"},"PeriodicalIF":0.0,"publicationDate":"2022-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/c4/cb/main.PMC9486134.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"33477535","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Manuka honey in combination with azithromycin shows potential for improved activity against Mycobacterium abscessus","authors":"Victoria C. Nolan,&nbsp;James Harrison,&nbsp;Jonathan A.G. Cox","doi":"10.1016/j.tcsw.2022.100090","DOIUrl":"10.1016/j.tcsw.2022.100090","url":null,"abstract":"<div><p><em>Mycobacterium abscessus</em> is an increasingly prevalent opportunistic pathogen causing both pulmonary and skin and soft tissue infections. It is of increasing concern for immunocompromised individuals, such as those with cystic fibrosis, due to its highly drug resistant nature and ability to evade the host immune system. Current treatments for <em>M. abscessus</em> pulmonary infections are largely ineffective and treatment outcomes are generally poor, thus we urgently require new treatments to combat these infections. Recently, it has been demonstrated that manuka honey is effective against <em>M. abscessus</em> and can improve the inhibitory effect of amikacin. Here, we explore the potential improvement of both azithromycin and tobramycin with the addition of manuka honey against <em>M. abscessus</em> complex. Improved growth inhibition was observed for azithromycin with manuka honey against all <em>M. abscessus</em> subspecies. Improved bactericidal activity was also observed. Importantly, the macrolide resistant <em>M. abscessus</em> subsp. <em>bolletii</em> showed improved inhibition and bactericidal activity was obtained in response to 0.117 g/mL manuka honey MGO40 with 16 µg/mL azithromycin. No improved activity was observed for tobramycin and manuka honey against any of the <em>M. abscessus</em> isolates tested. This demonstrates the potential for antibiotic enhancement by the addition of manuka honey, furthering the applications of therapeutic manuka honey.</p></div>","PeriodicalId":36539,"journal":{"name":"Cell Surface","volume":"8 ","pages":"Article 100090"},"PeriodicalIF":0.0,"publicationDate":"2022-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9703798/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40505858","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}