期刊
TRENDS IN MICROBIOLOGY
卷 23, 期 10, 页码 630-641出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.tim.2015.07.003
关键词
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资金
- Strategic Priority Research Program of the Chinese Academy of Sciences [XDB08020202]
- China National Science Foundation [31225002, 31461143006]
- National Basic Research Program of China 973 Programs [20120B518700, 2014CB849602]
- Howard Hughes Medical Institute
Pathogenic bacteria encode virulent glycosyltransferases that conjugate various glycans onto substrate proteins via the N- or O-linkage. The HMW system in nontypeable Haemophilus influenzae and the Pgl system in Campylobacter jejuni glycosylate bacterial surface or periplasmic proteins at the eukaryoticlike Asn-X-Ser/Thr motif. The NIeB effector from enterobacteria mediates arginine GIcNAcylation of host death-domain proteins to block inflammation, representing an atypical N-glycosylation. The large clostridial cytotoxins and related glucosyltransferase toxins from Legionella and Photorhabdus mono-glycosylate a serine/threonine or tyrosine in host Rho GTPase or elongation factor 1A (eEF1A). The emerging bacterial autotransporter heptosyltransferase (BAHT) family of heptosyltransferases also catalyses O-glycosylation and modifies autotransporters for adhesion to the host. These glycosylations, diverse in linkages and glycan structures, determine appropriate functioning of bacterial virulence factors or hijack host cellular processes in pathogenesis.
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