Cell Surface最新文献_第3页

Advances on cell wall biology: Highlights from the XVI Plant Cell Wall Meeting 细胞壁生物学研究进展：第十六届植物细胞壁会议要点

Cell Surface Pub Date : 2024-12-01 DOI: 10.1016/j.tcsw.2024.100130

Hugo Mélida , Antonio Molina

引用次数: 0

Antimicrobial peptides and proteins against drug-resistant pathogens 抗耐药性病原体的抗菌肽和蛋白质

Cell Surface Pub Date : 2024-12-01 DOI: 10.1016/j.tcsw.2024.100135

Yeji Wang, Minghui Song, Wenqiang Chang

{"title":"Antimicrobial peptides and proteins against drug-resistant pathogens","authors":"Yeji Wang, Minghui Song, 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}

引用次数: 0

Combatting biofilm-mediated infections in clinical settings by targeting quorum sensing 以法定人数感应为目标，抗击临床环境中生物膜介导的感染

Cell Surface Pub Date : 2024-11-08 DOI: 10.1016/j.tcsw.2024.100133

Arindam Mitra

{"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}

引用次数: 0

The role of ABC transporter DrrABC in the export of PDIM in Mycobacterium tuberculosis ABC 转运体 DrrABC 在结核分枝杆菌 PDIM 的输出过程中的作用

Cell Surface Pub Date : 2024-10-15 DOI: 10.1016/j.tcsw.2024.100132

Nabiela Moolla , Helen Weaver , Rebeca Bailo , Albel Singh , Vassiliy N. Bavro , Apoorva Bhatt

{"title":"The role of ABC transporter DrrABC in the export of PDIM in Mycobacterium tuberculosis","authors":"Nabiela Moolla , Helen Weaver , Rebeca Bailo , Albel Singh , Vassiliy N. Bavro , Apoorva Bhatt","doi":"10.1016/j.tcsw.2024.100132","DOIUrl":"10.1016/j.tcsw.2024.100132","url":null,"abstract":"<div><div>The <em>Mycobacterium tuberculosis</em> virulence lipid phthiocerol dimycocerosate (PDIM) is exported by a complex mechanism that involves multiple proteins including the Resistance-Nodulation-Division (RND) transporter MmpL7 and the lipoprotein LppX. Here, we probe the role of the putative heterooligomeric ATP-Binding Cassette (ABC) transporter complex composed of DrrA, DrrB and DrrC in PDIM transport by constructing a set of individual null mutants of <em>drrA</em>, <em>drrB</em> and <em>drrC</em> in the vaccine strain <em>Mycobacterium bovis</em> BCG. Loss of all three, or individual <em>drr</em> genes, all resulted in a complete loss of PDIM export to the outer envelope of the mycobacterial cell. Furthermore, guided by a bioinformatic analysis we interrogated specific signature residues within the DrrABC to demonstrate that it is indeed an ABC transporter, and our modelling, together with the mutagenesis identify it as a member of the Type V family of ABC exporters. We identify several unique structural elements of the transporter, including a non-canonical C-terminally inserted domain (CTD) structure within DrrA, which may account for its functional properties.</div></div>","PeriodicalId":36539,"journal":{"name":"Cell Surface","volume":"12 ","pages":"Article 100132"},"PeriodicalIF":0.0,"publicationDate":"2024-10-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142534922","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}

引用次数: 0

Sorting of GPI-anchored proteins at the trypanosome surface is independent of GPI insertion signals 锥虫表面 GPI-anchored 蛋白质的分拣与 GPI 插入信号无关

Cell Surface Pub Date : 2024-07-06 DOI: 10.1016/j.tcsw.2024.100131

Thomas Henry Miller, Sabine Schiessler, Ella Maria Rogerson, Catarina Gadelha

{"title":"Sorting of GPI-anchored proteins at the trypanosome surface is independent of GPI insertion signals","authors":"Thomas Henry Miller, Sabine Schiessler, Ella Maria Rogerson, Catarina Gadelha","doi":"10.1016/j.tcsw.2024.100131","DOIUrl":"10.1016/j.tcsw.2024.100131","url":null,"abstract":"<div><p>The segregation of glycosylphosphatidylinositol-anchored proteins (GPI-APs) to distinct domains on the plasma membrane of eukaryotic cells is important for their correct cellular function, but the mechanisms by which GPI-APs are sorted are yet to be fully resolved. An extreme example of this is in African trypanosomes, where the major surface glycoprotein floods the whole cell surface while most GPI-APs are retained in a specialised domain at the base of the flagellum. One possibility is that anchor attachment signals direct differential sorting of proteins. To investigate this, we fused a monomeric reporter to the GPI-anchor insertion signals of trypanosome proteins that are differentially sorted on the plasma membrane. Fusions were correctly anchored by GPI, post-translationally modified, and routed to the plasma membrane, but this delivery was independent of retained signals upstream of the ω site. Instead, ω−minus signal strength appears key to efficacy of GPI addition and to GPI-AP cellular level. Thus, at least in this system, sorting is not encoded at the time of GPI anchor addition or in the insertion sequence retained in processed proteins. We discuss these findings in the context of previously proposed models for sorting mechanisms in trypanosomes.</p></div>","PeriodicalId":36539,"journal":{"name":"Cell Surface","volume":"12 ","pages":"Article 100131"},"PeriodicalIF":0.0,"publicationDate":"2024-07-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2468233024000136/pdfft?md5=a9a844d450b03176be09a99639b5b69e&pid=1-s2.0-S2468233024000136-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141623033","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}

引用次数: 0

Study of fungal cell wall evolution through its monosaccharide composition: An insight into fungal species interacting with plants 通过单糖组成研究真菌细胞壁的进化：洞察与植物相互作用的真菌物种

Cell Surface Pub Date : 2024-06-01 DOI: 10.1016/j.tcsw.2024.100127

Sara I. Yugueros , Jorge Peláez , Jason E. Stajich , María Fuertes-Rabanal , Andrea Sánchez-Vallet , Asier Largo-Gosens , Hugo Mélida

{"title":"Study of fungal cell wall evolution through its monosaccharide composition: An insight into fungal species interacting with plants","authors":"Sara I. Yugueros , Jorge Peláez , Jason E. Stajich , María Fuertes-Rabanal , Andrea Sánchez-Vallet , Asier Largo-Gosens , Hugo Mélida","doi":"10.1016/j.tcsw.2024.100127","DOIUrl":"https://doi.org/10.1016/j.tcsw.2024.100127","url":null,"abstract":"<div><p>Every fungal cell is encapsulated in a cell wall, essential for cell viability, morphogenesis, and pathogenesis. Most knowledge of the cell wall composition in fungi has focused on ascomycetes, especially human pathogens, but considerably less is known about early divergent fungal groups, such as species in the Zoopagomycota and Mucoromycota phyla. To shed light on evolutionary changes in the fungal cell wall, we studied the monosaccharide composition of the cell wall of 18 species including early diverging fungi and species in the Basidiomycota and Ascomycota phyla with a focus on those with pathogenic lifestyles and interactions with plants. Our data revealed that chitin is the most characteristic component of the fungal cell wall, and was found to be in a higher proportion in the early divergent groups. The Mucoromycota species possess few glucans, but instead have other monosaccharides such as fucose and glucuronic acid that are almost exclusively found in their cell walls. Additionally, we observed that hexoses (glucose, mannose and galactose) accumulate in much higher proportions in species belonging to Dikarya. Our data demonstrate a clear relationship between phylogenetic position and fungal cell wall carbohydrate composition and lay the foundation for a better understanding of their evolution and their role in plant interactions.</p></div>","PeriodicalId":36539,"journal":{"name":"Cell Surface","volume":"11 ","pages":"Article 100127"},"PeriodicalIF":0.0,"publicationDate":"2024-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2468233024000094/pdfft?md5=f8770be407788d82bf7ccab067ae91f8&pid=1-s2.0-S2468233024000094-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141243527","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}

引用次数: 0

Impact of secreted glucanases upon the cell surface and fitness of Candida albicans during colonisation and infection 在定植和感染过程中，分泌葡聚糖酶对白色念珠菌细胞表面和适应性的影响

Cell Surface Pub Date : 2024-06-01 DOI: 10.1016/j.tcsw.2024.100128

Qinxi Ma , Arnab Pradhan , Ian Leaves , Emer Hickey , Elena Roselletti , Ivy Dambuza , Daniel E. Larcombe , Leandro Jose de Assis , Duncan Wilson , Lars P. Erwig , Mihai G. Netea , Delma S. Childers , Gordon D. Brown , Neil A.R. Gow , Alistair J.P. Brown

{"title":"Impact of secreted glucanases upon the cell surface and fitness of Candida albicans during colonisation and infection","authors":"Qinxi Ma , Arnab Pradhan , Ian Leaves , Emer Hickey , Elena Roselletti , Ivy Dambuza , Daniel E. Larcombe , Leandro Jose de Assis , Duncan Wilson , Lars P. Erwig , Mihai G. Netea , Delma S. Childers , Gordon D. Brown , Neil A.R. Gow , Alistair J.P. Brown","doi":"10.1016/j.tcsw.2024.100128","DOIUrl":"10.1016/j.tcsw.2024.100128","url":null,"abstract":"<div><p>Host recognition of the pathogen-associated molecular pattern (PAMP), β-1,3-glucan, plays a major role in antifungal immunity. β-1,3-glucan is an essential component of the inner cell wall of the opportunistic pathogen <em>Candida albicans</em>. Most β-1,3-glucan is shielded by the outer cell wall layer of mannan fibrils, but some can become exposed at the cell surface. In response to host signals such as lactate, <em>C. albicans</em> shaves the exposed β-1,3-glucan from its cell surface, thereby reducing the ability of innate immune cells to recognise and kill the fungus. We have used sets of barcoded <em>xog1</em> and <em>eng1</em> mutants to compare the impacts of the secreted β-glucanases Xog1 and Eng1 upon <em>C. albicans in vitro</em> and <em>in vivo</em>. Flow cytometry of Fc-dectin-1-stained strains revealed that Eng1 plays the greater role in lactate-induced β-1,3-glucan masking. Transmission electron microscopy and stress assays showed that neither Eng1 nor Xog1 are essential for cell wall maintenance, but the inactivation of either enzyme compromised fungal adhesion to gut and vaginal epithelial cells. Competitive barcode sequencing suggested that neither Eng1 nor Xog1 strongly influence <em>C. albicans</em> fitness during systemic infection or vaginal colonisation in mice. However, the deletion of <em>XOG1</em> enhanced <em>C. albicans</em> fitness during gut colonisation. We conclude that both Eng1 and Xog1 exert subtle effects on the <em>C. albicans</em> cell surface that influence fungal adhesion to host cells and that affect fungal colonisation in certain host niches.</p></div>","PeriodicalId":36539,"journal":{"name":"Cell Surface","volume":"11 ","pages":"Article 100128"},"PeriodicalIF":0.0,"publicationDate":"2024-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2468233024000100/pdfft?md5=65705da5b1785db1447a44b255bd78e8&pid=1-s2.0-S2468233024000100-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141275629","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}

引用次数: 0

Erratum to “Fungal cell wall components modulate our immune system” [Cell Surf. 7 (2021) 100067] 对《真菌细胞壁成分调节我们的免疫系统》的勘误 [Cell Surf.

Cell Surface Pub Date : 2024-06-01 DOI: 10.1016/j.tcsw.2024.100119

Benoit Briard , Thierry Fontaine , Thirumala-Devi Kanneganti , Neil A.R. Gow , Nicolas Papon

引用次数: 0

Powerful cell wall biomass degradation enzymatic system from saprotrophic Aspergillus fumigatus 腐生曲霉强大的细胞壁生物质降解酶系统

Cell Surface Pub Date : 2024-05-21 DOI: 10.1016/j.tcsw.2024.100126

Lige Tong , Yunaying Li , Xinke Lou , Bin Wang , Cheng Jin , Wenxia Fang

{"title":"Powerful cell wall biomass degradation enzymatic system from saprotrophic Aspergillus fumigatus","authors":"Lige Tong , Yunaying Li , Xinke Lou , Bin Wang , Cheng Jin , Wenxia Fang","doi":"10.1016/j.tcsw.2024.100126","DOIUrl":"https://doi.org/10.1016/j.tcsw.2024.100126","url":null,"abstract":"<div><p>Cell wall biomass, Earth’s most abundant natural resource, holds significant potential for sustainable biofuel production. Composed of cellulose, hemicellulose, lignin, pectin, and other polymers, the plant cell wall provides essential structural support to diverse organisms in nature. In contrast, non-plant species like insects, crustaceans, and fungi rely on chitin as their primary structural polysaccharide. The saprophytic fungus <em>Aspergillus fumigatus</em> has been widely recognized for its adaptability to various environmental conditions. It achieves this by secreting different cell wall biomass degradation enzymes to obtain essential nutrients. This review compiles a comprehensive collection of cell wall degradation enzymes derived from <em>A. fumigatus</em>, including cellulases, hemicellulases, various chitin degradation enzymes, and other polymer degradation enzymes. Notably, these enzymes exhibit biochemical characteristics such as temperature tolerance or acid adaptability, indicating their potential applications across a spectrum of industries.</p></div>","PeriodicalId":36539,"journal":{"name":"Cell Surface","volume":"11 ","pages":"Article 100126"},"PeriodicalIF":0.0,"publicationDate":"2024-05-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2468233024000082/pdfft?md5=4b3a2fb15bf2f3b050c9a7cf76d15337&pid=1-s2.0-S2468233024000082-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141089975","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}

引用次数: 0

Formative evaluation and structural analysis of non-tuberculosis mycobacterial biofilm using material pieces 利用材料碎片对非结核分枝杆菌生物膜进行形成性评估和结构分析

Cell Surface Pub Date : 2024-05-14 DOI: 10.1016/j.tcsw.2024.100125

Kentaro Yamamoto , Shota Torigoe , Hirotaka Kobayashi

引用次数: 0