Warren Matthew J, Roddam Louise F, Power Peter M, Terry Tamsin D, Jennings Michael P
Department of Microbiology and Parasitology, School of Molecular and Microbial Sciences, The University of Queensland, Brisbane, Qld 4072, Australia.
FEMS Immunol Med Microbiol. 2004 May 1;41(1):43-50. doi: 10.1016/j.femsim.2004.01.002.
Pilin is the major subunit of the essential virulence factor pili and is glycosylated at Ser63. In this study we investigated the gene pglI to determine whether it is involved in the biosynthesis of the pilin-linked glycan of Neisseria meningitidis strain C311#3. A N. meningitidis C311#3pglI mutant resulted in a change of apparent molecular weight in SDS-PAGE and altered binding of antisera, consistent with a role in the biosynthesis of the pilin-linked glycan. These data, in conjunction with homology with well-characterised acyltransferases suggests a specific role for pglI in the biosynthesis of the basal 2,4-diacetamido-2,4,6-trideoxyhexose residue of the pilin-linked glycan.
菌毛蛋白是必需毒力因子菌毛的主要亚基，且在丝氨酸63处发生糖基化。在本研究中，我们对基因pglI进行了研究，以确定其是否参与脑膜炎奈瑟菌C311#3菌株菌毛连接聚糖的生物合成。脑膜炎奈瑟菌C311#3 pglI突变体导致SDS-PAGE中表观分子量发生变化，并改变了抗血清的结合，这与它在菌毛连接聚糖生物合成中的作用一致。这些数据，连同与特征明确的酰基转移酶的同源性，表明pglI在菌毛连接聚糖的基础2,4-二乙酰氨基-2,4,6-三脱氧己糖残基的生物合成中具有特定作用。
