Cell Surface最新文献

{"title":"The role of triacylglycerols and repurposing DGAT1 inhibitors for the treatment of Mycobacterium tuberculosis","authors":"Alice R. Moorey,&nbsp;Gurdyal S. Besra","doi":"10.1016/j.tcsw.2022.100083","DOIUrl":"10.1016/j.tcsw.2022.100083","url":null,"abstract":"<div><p>Latent tuberculosis poses a significant threat to global health through the incubation of undiagnosed infections within the community, and through its tolerance to antibiotics. This Special Features article explores the mechanisms by which the dormant <em>Mycobacterium tuberculosis</em> pathogen can store energy in the form of lipid inclusion bodies and triacylglycerols, which may be key in the development of novel therapeutics to treat TB.</p></div>","PeriodicalId":36539,"journal":{"name":"Cell Surface","volume":"8 ","pages":"Article 100083"},"PeriodicalIF":0.0,"publicationDate":"2022-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9578982/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"10803214","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":"Post-transcriptional control of fungal cell wall synthesis","authors":"Rebecca A. Hall ,&nbsp;Edward W.J. Wallace","doi":"10.1016/j.tcsw.2022.100074","DOIUrl":"10.1016/j.tcsw.2022.100074","url":null,"abstract":"<div><p>Pathogenic fungi hide from their hosts by camouflage, obscuring immunogenic cell wall components such as beta-glucan with innocuous coverings such as mannoproteins and alpha-glucan that are less readily recognised by the host. Attempts to understand how such processes are regulated have met with varying success. Typically studies focus on understanding the transcriptional response of fungi to either their reservoir environment or the host. However, such approaches do not fully address this research question, due to the layers of post-transcriptional and post-translational regulation that occur within a cell. Although in animals the impact of post-transcriptional and post-translational regulation has been well characterised, our knowledge of these processes in the fungal kingdom is more limited. Mutations in RNA-binding proteins, like Ssd1 and <em>Candida albicans</em> Slr1, affect cell wall composition and fungal virulence indicating that post-transcriptional regulation plays a key role in these processes. Here, we review the current state of knowledge of fungal post-transcriptional regulation, and link this to potential mechanisms of immune evasion by drawing on studies from model yeast and plant pathogenic fungi. We highlight several RNA-binding proteins that regulate cell wall synthesis and could be involved in local translation of cell wall components. Expanding our knowledge on post-transcriptional regulation in human fungal pathogens is essential to fully comprehend fungal virulence strategies and for the design of novel antifungal therapies.</p></div>","PeriodicalId":36539,"journal":{"name":"Cell Surface","volume":"8 ","pages":"Article 100074"},"PeriodicalIF":0.0,"publicationDate":"2022-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8783092/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39750419","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":"In silico identification of Theileria parva surface proteins","authors":"Nitisha Gurav ,&nbsp;Olivia J.S. Macleod ,&nbsp;Paula MacGregor ,&nbsp;R. Ellen R. Nisbet","doi":"10.1016/j.tcsw.2022.100078","DOIUrl":"10.1016/j.tcsw.2022.100078","url":null,"abstract":"<div><p>East Coast Fever is a devastating African cattle disease caused by the apicomplexan parasite, <em>Theileria parva</em>. Little is known about the cell surface, and few proteins have been identified. Here, we take an <em>in silico</em> approach to identify novel cell surface proteins, and predict the structure of four key proteins.</p></div>","PeriodicalId":36539,"journal":{"name":"Cell Surface","volume":"8 ","pages":"Article 100078"},"PeriodicalIF":0.0,"publicationDate":"2022-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S246823302200007X/pdfft?md5=f4380bf9157180772cca7a2cd712aa3e&pid=1-s2.0-S246823302200007X-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"45753526","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":"Detecting the orientation of newly-deposited crystalline cellulose with fluorescent CBM3","authors":"Sarah A. Pfaff,&nbsp;Xuan Wang,&nbsp;Edward R. Wagner,&nbsp;Liza A. Wilson,&nbsp;Sarah N. Kiemle,&nbsp;Daniel J. Cosgrove","doi":"10.1016/j.tcsw.2022.100089","DOIUrl":"10.1016/j.tcsw.2022.100089","url":null,"abstract":"<div><p>Cellulose microfibril patterning influences many of the mechanical attributes of plant cell walls. We developed a simple, fluorescence microscopy-based method to detect the orientation of newly-synthesized cellulose microfibrils in epidermal peels of onion and Arabidopsis. It is based on Alexa Fluor 488-tagged carbohydrate binding module 3a (CBM3a) from <em>Clostridium thermocellum</em> which displayed a nearly 4-fold greater binding to cell walls at pH 5.5 compared with pH 8. Binding to isolated cellulose did not display this pH dependence. At pH 7.5 fibrillar patterns at the surface of the epidermal peels were visible, corresponding to the directionality of surface cellulose microfibrils, as verified by atomic force microscopy. The fibrillar pattern was not visible as the labeling intensity increased at lower pH. The pH of greatest cell wall labeling corresponds to the isoelectric point of CBM3a, suggesting that electrostatic forces limit CBM3a penetration into the wall. Consistent with this, digestion of the wall with pectate lyase to remove homogalacturonan increased labeling intensity. We conclude that electrostatic interactions strongly influence labeling of cell walls with CBM3 and potentially other proteins, holding implications for any work that relies on penetration of protein probes such as CBMs, antibodies, or enzymes into charged polymeric substrates.</p></div>","PeriodicalId":36539,"journal":{"name":"Cell Surface","volume":"8 ","pages":"Article 100089"},"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/5f/b7/main.PMC9678952.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40706891","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":"Polygalacturonase activity promotes aberrant cell separation in the quasimodo2 mutant of Arabidopsis thaliana","authors":"William J. Barnes ,&nbsp;Ellen Zelinsky ,&nbsp;Charles T. Anderson","doi":"10.1016/j.tcsw.2021.100069","DOIUrl":"10.1016/j.tcsw.2021.100069","url":null,"abstract":"<div><p>In plants, cell adhesion relies on balancing the integrity of the pectin-rich middle lamella with wall loosening during tissue expansion. Mutation of <em>QUASIMODO2</em> (<em>QUA2</em>), a pectin methyltransferase, causes defective hypocotyl elongation and cell adhesion in <em>Arabidopsis thaliana</em> hypocotyls<em>.</em> However, the molecular function of QUA2 in cell adhesion is obscured by complex genetic and environmental interactions. To dissect the role of QUA2 in cell adhesion, we investigated a <em>qua2</em> loss-of-function mutant and a suppressor mutant with restored cell adhesion, <em>qua2 esmeralda1</em>, using a combination of imaging and biochemical techniques. We found that <em>qua2</em> hypocotyls have reductions in middle lamellae integrity, pectin methyl-esterase (PME) activity, pectin content and molecular mass, and immunodetected Ca²⁺-crosslinking at cell corners, but increased methyl-esterification and polygalacturonase (PG) activity, with <em>qua2 esmd1</em> having wild type-like or intermediate phenotypes. Our findings suggest that excessive pectin degradation prevents pectin accumulation and the formation of a sufficiently Ca²⁺-crosslinked network to maintain cell adhesion in <em>qua2</em> mutants. We propose that PME and PG activities balance tissue-level expansion and cell separation. Together, these data provide insight into the cause of cell adhesion defects in <em>qua2</em> mutants and highlight the importance of harmonizing pectin modification and degradation during plant growth and development.</p></div>","PeriodicalId":36539,"journal":{"name":"Cell Surface","volume":"8 ","pages":"Article 100069"},"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/73/4b/main.PMC8686065.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39657395","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":"Ending the (Cell) wall metaphor in microbiology","authors":"Arturo Casadevall ,&nbsp;Neil A.R. Gow","doi":"10.1016/j.tcsw.2022.100087","DOIUrl":"10.1016/j.tcsw.2022.100087","url":null,"abstract":"","PeriodicalId":36539,"journal":{"name":"Cell Surface","volume":"8 ","pages":"Article 100087"},"PeriodicalIF":0.0,"publicationDate":"2022-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9668729/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"10803805","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":"Impact of changes at the Candida albicans cell surface upon immunogenicity and colonisation in the gastrointestinal tract","authors":"Gabriela M. Avelar ,&nbsp;Ivy M. Dambuza ,&nbsp;Liviana Ricci ,&nbsp;Raif Yuecel ,&nbsp;Kevin Mackenzie ,&nbsp;Delma S. Childers ,&nbsp;Judith M. Bain ,&nbsp;Arnab Pradhan ,&nbsp;Daniel E. Larcombe ,&nbsp;Mihai G. Netea ,&nbsp;Lars P. Erwig ,&nbsp;Gordon D. Brown ,&nbsp;Sylvia H. Duncan ,&nbsp;Neil A.R. Gow ,&nbsp;Alan W. Walker ,&nbsp;Alistair J.P. Brown","doi":"10.1016/j.tcsw.2022.100084","DOIUrl":"10.1016/j.tcsw.2022.100084","url":null,"abstract":"<div><p>The immunogenicity of <em>Candida albicans</em> cells is influenced by changes in the exposure of microbe-associated molecular patterns (MAMPs) on the fungal cell surface. Previously, the degree of exposure on the <em>C. albicans</em> cell surface of the immunoinflammatory MAMP β-(1,3)-glucan was shown to correlate inversely with colonisation levels in the gastrointestinal (GI) tract. This is important because life-threatening systemic candidiasis in critically ill patients often arises from translocation of <em>C. albicans</em> strains present in the patient’s GI tract. Therefore, using a murine model, we have examined the impact of gut-related factors upon β-glucan exposure and colonisation levels in the GI tract.</p><p>The degree of β-glucan exposure was examined by imaging flow cytometry of <em>C. albicans</em> cells taken directly from GI compartments, and compared with colonisation levels. Fungal β-glucan exposure was lower in the cecum than the small intestine, and fungal burdens were correspondingly higher in the cecum. This inverse correlation did not hold for the large intestine.</p><p>The gut fermentation acid, lactate, triggers β-glucan masking <em>in vitro,</em> leading to attenuated anti-<em>Candida</em> immune responses. Additional fermentation acids are present in the GI tract, including acetate, propionate, and butyrate. We show that these acids also influence β-glucan exposure on <em>C. albicans</em> cells <em>in vitro</em> and, like lactate, they influence β-glucan exposure via Gpr1/Gpa2-mediated signalling. Significantly, <em>C. albicans gpr</em>1Δ <em>gpa</em>2Δ cells displayed elevated β-glucan exposure in the large intestine and a corresponding decrease in fungal burden, consistent with the idea that Gpr1/Gpa2-mediated β-glucan masking influences colonisation of this GI compartment. Finally, extracts from the murine gut and culture supernatants from the mannan grazing gut anaerobe <em>Bacteroides thetaiotaomicron</em> promote β-glucan exposure at the <em>C. albicans</em> cell surface. Therefore, the local microbiota influences β-glucan exposure levels directly (via mannan grazing) and indirectly (via fermentation acids), whilst β-glucan masking appears to promote <em>C. albicans</em> colonisation of the murine large intestine.</p></div>","PeriodicalId":36539,"journal":{"name":"Cell Surface","volume":"8 ","pages":"Article 100084"},"PeriodicalIF":0.0,"publicationDate":"2022-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9589014/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9176657","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":"Virulence factors of uropathogens and their role in host pathogen interactions","authors":"Deenadayalan Karaiyagowder Govindarajan,&nbsp;Kumaravel Kandaswamy","doi":"10.1016/j.tcsw.2022.100075","DOIUrl":"10.1016/j.tcsw.2022.100075","url":null,"abstract":"<div><p>Gram-positive and Gram-negative<!--> <!-->bacterial pathogens are commonly found in Urinary Tract Infection (UTI), particularly infected in females like pregnant women, elder people, sexually active, or individuals prone to other risk factors for UTI. In this article, we review the expression of virulence surface proteins and their interaction with host cells for the most frequently isolated uropathogens: <em>Escherichia coli</em>, <em>Enterococcus faecalis, Proteus mirabilis</em>, <em>Klebsiella pneumoniae</em>, and <em>Staphylococcus saprophyticus</em>. In addition to the host cell interaction, surface protein regulation was also discussed in this article. The surface protein regulation serves as a key tool in differentiating the pathogen isotypes. Furthermore, it might provide insights on novel diagnostic methods to detect uropathogen that are otherwise easily overlooked due to limited culture-based assays. In essence, this review shall provide an in-depth understanding on secretion of virulence factors of various uropathogens and their role in host-pathogen interaction, this knowledge might be useful in the development of therapeutics against uropathogens.</p></div>","PeriodicalId":36539,"journal":{"name":"Cell Surface","volume":"8 ","pages":"Article 100075"},"PeriodicalIF":0.0,"publicationDate":"2022-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8841375/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39645498","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":"Enhanced immunogenicity of Mycobacterium bovis BCG through CRISPRi mediated depletion of AftC","authors":"Bala T.S.A. Madduri ,&nbsp;Lauren Allen ,&nbsp;Stephen C. Taylor ,&nbsp;Gurdyal S. Besra ,&nbsp;Luke J. Alderwick","doi":"10.1016/j.tcsw.2022.100088","DOIUrl":"10.1016/j.tcsw.2022.100088","url":null,"abstract":"<div><p><em>Mycobacterium tuberculosis</em> causes the disease tuberculosis and affects a third of the world’s population. The recent COVID-19 pandemic exacerbated the situation with a projected 27% increase in tuberculosis related deaths. <em>M. tuberculosis</em> has an elaborate cell wall consisting of peptidoglycan, arabinogalactan and mycolic acids which shield the bacilli from the toxic bactericidal <em>milieu</em> within phagocytes. Amongst, the numerous glycosyltransferase enzymes involved in mycobacterial cell wall biosynthesis, arabinofuranosyltransferase C (<em>aftC</em>) is responsible for the branching of the arabinan domain in both arabinogalactan and lipoarabinomannan. Using Clustered Regularly Interspaced Short Palindromic Repeats interference (CRISPRi) we have generated <em>aftC</em> knockdowns in <em>Mycobacterium bovis</em> BCG and demonstrated the generation of a truncated, immunogenic lipoarabinomannan within its cell envelope. The <em>aftC</em> depleted BCG mutants were unable to form characteristic mycobacterial pellicular biofilms and elicit a potent immunostimulatory phenotype compared to wild type <em>M. bovis</em> BCG in a THP1 cell line. This study paves the way to further explore novel BCG mutants as promising vaccine boosters in preventing pulmonary tuberculosis.</p></div>","PeriodicalId":36539,"journal":{"name":"Cell Surface","volume":"8 ","pages":"Article 100088"},"PeriodicalIF":0.0,"publicationDate":"2022-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9651938/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40477806","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":"Phosphocholine decoration of Proteus mirabilis O18 LPS induces hydrophobicity of the cell surface and electrokinetic potential, but does not alter the adhesion to solid surfaces","authors":"Grzegorz Czerwonka ,&nbsp;Katarzyna Durlik-Popińska ,&nbsp;Marcin Drabik ,&nbsp;Martyna Szczerba ,&nbsp;Maria Kwiatkowska ,&nbsp;Wiesław Kaca","doi":"10.1016/j.tcsw.2022.100079","DOIUrl":"10.1016/j.tcsw.2022.100079","url":null,"abstract":"<div><p><em>Proteus mirabilis</em> harbours a variety of O antigens, permitting evasion of the host immune response. LPS decoration with phosphocholine increases cell surface hydrophobicity and decreases electrokinetic potential, which may interfere with antibody interaction and bacterial surface recognition. The decoration does not influence adherence to solid surfaces.</p></div>","PeriodicalId":36539,"journal":{"name":"Cell Surface","volume":"8 ","pages":"Article 100079"},"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/19/10/main.PMC9213243.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40401939","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}