Cell Surface最新文献

{"title":"Comprehensive phenotypic analysis of multiple gene deletions of α-glucan synthase and Crh-transglycosylase gene families in Aspergillus niger highlighting the versatility of the fungal cell wall","authors":"Katharina J. Ost ,&nbsp;Mark Arentshorst ,&nbsp;Bruno M. Moerschbacher ,&nbsp;Mareike E. Dirks-Hofmeister ,&nbsp;Arthur F.J. Ram","doi":"10.1016/j.tcsw.2025.100141","DOIUrl":"10.1016/j.tcsw.2025.100141","url":null,"abstract":"<div><div>Multiple paralogs are found in the fungal genomes for several genes that encode proteins involved in cell wall biosynthesis. The genome of <em>A. niger</em> contains five genes encoding putative α-1,3-glucan synthases (AgsA-E) and seven genes encoding putative glucan-chitin crosslinking enzymes (CrhA-G). Here, we systematically studied the effects of the deletion of single (<em>agsA</em> or <em>agsE</em>), double (<em>agsA</em> and <em>agsE)</em>, or all five <em>ags</em> genes (<em>agsA-E</em>) present in <em>A. niger</em>. Morphological and biochemical analysis of <em>ags</em> mutants emphasizes the important role of <em>agsE</em> in cell wall integrity, while deletion of other <em>ags</em> genes had minimal impact. Loss of <em>agsE</em> compromised cell wall integrity and altered pellet morphology in liquid cultures.</div><div>Previous studies have indicated that deletion of all <em>crh</em> genes in <em>A. niger</em> did not result in cell wall integrity-related phenotypes. To determine whether the <em>ags</em> and <em>crh</em> gene families have redundant functions, both gene families were deleted using iterative CRISPR/Cas9 mediated genome editing. The 12-fold deletion mutant was viable and did not exhibit growth defects under non-stressing growth conditions. A synergistic effect on cell wall integrity was observed in this 12-fold deletion mutant, particularly when exposed to cell wall-perturbing compounds. The cell wall composition, extractability of glucans by alkali, and scanning electron microscopy analysis showed no differences between the parental strain and mutants lacking <em>ags</em> genes, <em>crh</em> genes, or both. These observations underscore the ability of fungal cells to adapt and secure cell wall integrity, even when two entire cell wall protein-encoding gene families are missing.</div></div>","PeriodicalId":36539,"journal":{"name":"Cell Surface","volume":"13 ","pages":"Article 100141"},"PeriodicalIF":0.0,"publicationDate":"2025-01-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143301060","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":"Sporothrix brasiliensis Gp70 is a cell wall protein required for adhesion, proper interaction with innate immune cells, and virulence","authors":"Leonardo Padró-Villegas ,&nbsp;Manuela Gómez-Gaviria ,&nbsp;Iván Martínez-Duncker ,&nbsp;Luz A. López-Ramírez ,&nbsp;José A. Martínez-Álvarez ,&nbsp;Gustavo A. Niño-Vega ,&nbsp;Héctor M. Mora-Montes","doi":"10.1016/j.tcsw.2024.100139","DOIUrl":"10.1016/j.tcsw.2024.100139","url":null,"abstract":"<div><div><em>Sporothrix brasiliensis</em> is one of the leading etiological agents of sporotrichosis, a cutaneous and subcutaneous mycosis worldwide distributed. This organism has been recently associated with epidemic outbreaks in Brazil. Despite the medical relevance of this species, little is known about its virulence factors, and most of the information on this subject is extrapolated from <em>Sporothrix schenckii</em>. Here, we generated <em>S. brasiliensis</em> mutants, where <em>GP70</em> was silenced. In <em>S. schenckii</em>, this gene encodes a glycoprotein with adhesive properties required for virulence. The <em>S. brasiliensis GP70</em> silencing led to an abnormal cellular phenotype, with smaller, round yeast-like cells that aggregate. Cell aggregation was disrupted with glucanase, suggesting this phenotype is linked to changes in the cell wall. The cell wall characterization confirmed changes in the structural polysaccharide β-1,3-glucan, which increased in quantity and exposure at the cell surface. This was accompanied by a reduction in protein content and <em>N</em>-linked glycans. Mutant strains with high <em>GP70</em>-silencing levels showed minimal levels of 3-carboxy-cis,cis-muconate cyclase activity, this glycoprotein's predicted enzyme function, and decreased ability to bind laminin and fibronectin. These phenotypical changes coincided with abnormal interaction with human peripheral blood mononuclear cells, where production of IL-1β, IL-17, and IL-22 was reduced and the strong dependence on cytokine stimulation <em>via</em> mannose receptor was lost. Phagocytosis by monocyte-derived macrophages was increased and virulence attenuated in a <em>Galleria mellonella</em> larvae. In conclusion, Gp70 is an abundant cell wall glycoprotein in <em>S. brasiliensis</em> that contributes to virulence and proper interaction with innate immnune cells.</div></div>","PeriodicalId":36539,"journal":{"name":"Cell Surface","volume":"13 ","pages":"Article 100139"},"PeriodicalIF":0.0,"publicationDate":"2025-01-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11763198/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143048180","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":"Characterization of the Neurospora crassa GH72 family of Laminarin/Lichenin transferases and their roles in cell wall biogenesis","authors":"Apurva Chatrath,&nbsp;Pavan Patel,&nbsp;Protyusha Dey,&nbsp;Stephen J. Free","doi":"10.1016/j.tcsw.2024.100140","DOIUrl":"10.1016/j.tcsw.2024.100140","url":null,"abstract":"<div><div>In <em>Neurospora crassa</em> vegetative hyphae, chitin, β-1,3-glucan (laminarin), and a mixed β-1,3−/β-1,4-glucan (lichenin) are the major cell wall polysaccharides. GH72 enzymes have been shown to function as β-1,3-glucanases and glucanosyltransferases and can function in crosslinking β-1,3-glucans together. To characterize the enzymatic activities of the <em>N. crassa</em> enzymes, we expressed GEL-1 with a HIS6 tag in <em>N. crassa.</em> A chimeric maltose binding protein:GEL-2 was produced in <em>E. coli</em>. Purified GEL-1 and GEL-2 were used to characterize their enzymatic activities. We employed thin-layer chromatography (TLC) and polyacrylamide carbohydrate gel electrophoresis (PACE) assays to visualize GEL-1 and GEL-2 hydrolase and transferase activities on lichenin and laminarin substrates. We determined that GEL-1 functions as a laminarinase (β-1,3-glucanase) and as a laminarin transferase. We found that GEL-2 can function as a laminarinase and as a licheninase (β-1,3−/β-1,4-mixed-glucanase) and can crosslink β-1,3-glucans together. We demonstrated that GEL-2 can form enzyme:lichenin intermediates, providing evidence that GEL-2 functions as a lichenin transferase as well as a β-1,3-glucan transferase and crosslinks both types of polysaccharides into the <em>N. crassa</em> cell wall.</div></div>","PeriodicalId":36539,"journal":{"name":"Cell Surface","volume":"13 ","pages":"Article 100140"},"PeriodicalIF":0.0,"publicationDate":"2025-01-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11758075/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143047334","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":"Endocytic tethers modulate unconventional GAPDH secretion","authors":"Michael J. Cohen ,&nbsp;Brianne Philippe ,&nbsp;Peter N. Lipke","doi":"10.1016/j.tcsw.2024.100138","DOIUrl":"10.1016/j.tcsw.2024.100138","url":null,"abstract":"<div><div>Yeast cell walls contain both classically-secreted and unconventionally-secreted proteins. The latter class lacks the signal sequence for translocation into the ER, therefore these proteins are transported to the wall by uncharacterized mechanisms. One such protein is the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH) which is abundant in the cytosol, but also found in the yeast cell wall where it is enzymatically active. We screened diploid <em>Saccharomyces cerevisiae</em> homozygous gene deletions for changes in cell wall GAPDH activity. Deletions targeting endocytic tethers in the endolysosomal system had the largest effects on GAPDH secretion, including <em>vps21, bro1, vps41, and pep12</em>. The predominant GAPDH isoform Tdh3 was partially localized to endolysosomal compartments, including multivesicular bodies, which are common entry points to unconventional protein secretion pathways. Yeast lacking the endosomal Rab5-GTPase Vps21 had defects in GAPDH secretion as well as delayed entry into to the endolysosomal compartments. Therefore, we conclude that entry into the endolysosomal compartment facilitates non-conventional secretion of GAPDH.</div></div>","PeriodicalId":36539,"journal":{"name":"Cell Surface","volume":"13 ","pages":"Article 100138"},"PeriodicalIF":0.0,"publicationDate":"2024-12-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11742311/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143013387","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":"Mucilicious methods: Navigating the tools developed to Arabidopsis Seed Coat Mucilage analysis","authors":"Susana Saez-Aguayo ,&nbsp;Dayan Sanhueza ,&nbsp;Vicente Jara ,&nbsp;Benjamin Galleguillos ,&nbsp;Alfonso Gonzalo de la Rubia ,&nbsp;Asier Largo-Gosens ,&nbsp;Adrian Moreno","doi":"10.1016/j.tcsw.2024.100134","DOIUrl":"10.1016/j.tcsw.2024.100134","url":null,"abstract":"<div><div>During the last decades, Arabidopsis seed mucilage has been extensively studied to gain insight into the metabolism of pectin, hemicellulose and cellulose. This review aims to provide a comprehensive examination of the techniques used to understand the composition and structure of <em>Arabidopsis</em> mucilage. Moreover, we present novel findings from mucilage analysis, including the separation of pectic domains within the mucilage, offering a fresh perspective on utilizing traditional techniques to analyze mucilage mutant lines.</div></div>","PeriodicalId":36539,"journal":{"name":"Cell Surface","volume":"13 ","pages":"Article 100134"},"PeriodicalIF":0.0,"publicationDate":"2024-12-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11696855/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142932907","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":"Staphylococcus aureus: Current perspectives on molecular pathogenesis and virulence","authors":"Abayeneh Girma","doi":"10.1016/j.tcsw.2024.100137","DOIUrl":"10.1016/j.tcsw.2024.100137","url":null,"abstract":"<div><div><em>Staphylococcus aureus</em> has evolved a sophisticated regulatory system to control its virulence. One of the main roles of this interconnected network is to sense and respond to diverse environmental signals by altering the synthesis of virulence components required for survival in the host, including cell surface adhesins, extracellular enzymes and toxins. The accessory gene regulator (agr), a quorum sensing system that detects the local concentration of a cyclic peptide signaling molecule, is one of the well-studied of these <em>S</em>. <em>aureus</em> regulatory mechanisms. By using this system, S. aureus is able to sense its own population density and translate this information into a specific pattern of gene expression. In addition to Agr, this pathogen senses specific stimuli through various two-component systems and synchronizes responses with alternative sigma factors and cytoplasmic regulators of the SarA protein family. These different regulatory mechanisms combine host and environmental information into a network that guarantees the best possible response of pathogens to changing circumstances. In this article, an overview of the most significant and thoroughly studied regulatory systems of <em>S</em>. <em>aureus</em> is provided, along with a summary of their roles in host interactions.</div></div>","PeriodicalId":36539,"journal":{"name":"Cell Surface","volume":"13 ","pages":"Article 100137"},"PeriodicalIF":0.0,"publicationDate":"2024-12-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11699754/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142932905","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":"Spatiotemporal regulation of alginate sub-structures at multiple scales revealed by monoclonal antibodies","authors":"Catherine T. Jones ,&nbsp;Cassie Bakshani ,&nbsp;Ieva Lelenaite ,&nbsp;Jozef Mravec ,&nbsp;Stjepan Krešimir Kračun ,&nbsp;Jeff Pearson ,&nbsp;Mathew D. Wilcox ,&nbsp;Kevin Hardouin ,&nbsp;Sonia Kridi ,&nbsp;Cécile Hervé ,&nbsp;William G.T. Willats","doi":"10.1016/j.tcsw.2024.100136","DOIUrl":"10.1016/j.tcsw.2024.100136","url":null,"abstract":"<div><div>Alginates are abundant linear polysaccharides produced by brown algae and some bacteria. They have multiple biological roles and important medical and commercial uses. Alginates are comprised of D-mannuronic acid (M) and L-guluronic acid (G) and the ratios and distribution patterns of M and G profoundly impact their physiological and rheological properties. The structure/function relationships of alginates have been extensively studied in vitro but our understanding of the in vivo spatiotemporal regulation of alginate fine structures and their biological implications is limited. Monoclonal antibodies (mAbs) are powerful tools for localising and quantifying glycan structures and several alginate-directed mAbs have been developed. We used a library of well-defined alginates, with M and G block ratios determined by NMR, to refine our understanding of the binding properties of alginate-directed mAbs. Using these probes, we obtained new insight into how structural features of alginates are regulated at different scales, from cellular to seasonal.</div></div>","PeriodicalId":36539,"journal":{"name":"Cell Surface","volume":"13 ","pages":"Article 100136"},"PeriodicalIF":0.0,"publicationDate":"2024-12-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11755070/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143030014","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":"Antimicrobial peptides and proteins against drug-resistant pathogens","authors":"Yeji Wang,&nbsp;Minghui Song,&nbsp;Wenqiang Chang","doi":"10.1016/j.tcsw.2024.100135","DOIUrl":"10.1016/j.tcsw.2024.100135","url":null,"abstract":"<div><div>The rise of drug-resistant pathogens, driven by the misuse and overuse of antibiotics, has created a formidable challenge for global public health. Antimicrobial peptides and proteins have garnered considerable attention as promising candidates for novel antimicrobial agents. These bioactive molecules, whether derived from natural sources, designed synthetically, or predicted using artificial intelligence, can induce lethal effects on pathogens by targeting key microbial structures or functional components, such as cell membranes, cell walls, biofilms, and intracellular components. Additionally, they may enhance overall immune defenses by modulating innate or adaptive immune responses in the host. Of course, development of antimicrobial peptides and proteins also face some limitations, including high toxicity, lack of selectivity, insufficient stability, and potential immunogenicity. Despite these challenges, they remain a valuable resource in the fight against drug-resistant pathogens. Future research should focus on overcoming these limitations to fully realize the therapeutic potential of antimicrobial peptides in the infection control.</div></div>","PeriodicalId":36539,"journal":{"name":"Cell Surface","volume":"12 ","pages":"Article 100135"},"PeriodicalIF":0.0,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142746995","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":"Advances on cell wall biology: Highlights from the XVI Plant Cell Wall Meeting","authors":"Hugo Mélida ,&nbsp;Antonio Molina","doi":"10.1016/j.tcsw.2024.100130","DOIUrl":"10.1016/j.tcsw.2024.100130","url":null,"abstract":"","PeriodicalId":36539,"journal":{"name":"Cell Surface","volume":"12 ","pages":"Article 100130"},"PeriodicalIF":0.0,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141702587","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":"Combatting biofilm-mediated infections in clinical settings by targeting quorum sensing","authors":"Arindam Mitra","doi":"10.1016/j.tcsw.2024.100133","DOIUrl":"10.1016/j.tcsw.2024.100133","url":null,"abstract":"<div><div>Biofilm-associated infections constitute a significant challenge in managing infectious diseases due to their high resistance to antibiotics and host immune responses. Biofilms are responsible for various infections, including urinary tract infections, cystic fibrosis, dental plaque, bone infections, and chronic wounds. Quorum sensing (QS) is a process of cell-to-cell communication that bacteria use to coordinate gene expression in response to cell density, which is crucial for biofilm formation and maintenance.. Its disruption has been proposed as a potential strategy to prevent or treat biofilm-associated infections leading to improved treatment outcomes for infectious diseases. This review article aims to provide a comprehensive overview of the literature on QS-mediated disruption of biofilms for treating infectious diseases. It will discuss the mechanisms of QS disruption and the various approaches that have been developed to disrupt QS in reference to multiple clinical pathogens. In particular, numerous studies have demonstrated the efficacy of QS disruption in reducing biofilm formation in various pathogens, including <em>Pseudomonas aeruginosa</em> and <em>Staphylococcus aureus</em>. Finally, the review will discuss the challenges and future directions for developing QS disruption as a clinical therapy for biofilm-associated infections. This includes the development of effective delivery systems and the identification of suitable targets for QS disruption. Overall, the literature suggests that QS disruption is a promising alternative to traditional antibiotic treatment for biofilm-associated infections and warrants further investigation.</div></div>","PeriodicalId":36539,"journal":{"name":"Cell Surface","volume":"12 ","pages":"Article 100133"},"PeriodicalIF":0.0,"publicationDate":"2024-11-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142660225","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}