Alm R A, Mattick J S
Centre for Molecular and Cellular Biology, University of Queensland, Brisbane, Australia.
Mol Microbiol. 1995 May;16(3):485-96. doi: 10.1111/j.1365-2958.1995.tb02413.x.
Type 4 fimbriae are important colonization factors in Pseudomonas aeruginosa and other pathogens that mediate attachment to epithelial cells of the host. They are also responsible for a form of translocation termed 'twitching motility' and are implicated in the susceptibility to fimbrial-specific bacteriophage. Analysis of a transposon mutant which lacks functional fimbriae has identified a new gene which is required for fimbrial biogenesis. This gene, termed pilV, is located on chromosomal SpeI fragment E, 2 kb downstream of the previously characterized pilSR genes involved in transcriptional activation of the fimbrial subunit gene. The pilV gene encodes a 20 kDa membrane-located protein with considerable amino-terminal homology to the type 4 consensus pre-pilin leader sequence, suggesting that it is processed by a leader peptidase. Site-directed mutagenesis has shown that PilV requires such cleavage to be functional. PilV also exhibits close similarity to a group of proteins involved in extracellular protein secretion from a number of Gram-negative bacteria, suggesting that the biogenesis of type 4 fimbriae may have a similar basis.
4型菌毛是铜绿假单胞菌和其他病原体中的重要定植因子,介导与宿主上皮细胞的附着。它们还负责一种称为“颤动运动”的移位形式,并与菌毛特异性噬菌体的易感性有关。对缺乏功能性菌毛的转座子突变体的分析鉴定出一个菌毛生物合成所需的新基因。这个基因称为pilV,位于染色体SpeI片段E上,在先前表征的参与菌毛亚基基因转录激活的pilSR基因下游2 kb处。pilV基因编码一种20 kDa的膜定位蛋白,其氨基末端与4型共有菌毛前体蛋白前导序列有相当的同源性,表明它是由前导肽酶加工的。定点诱变表明,PilV需要这种切割才能发挥功能。PilV还与许多革兰氏阴性细菌中参与细胞外蛋白分泌的一组蛋白质表现出密切相似性,这表明4型菌毛的生物合成可能有类似的基础。