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Microbiology 151 (2005), 3469-3482; DOI  10.1099/mic.0.28326-0
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Microbiology 151 (2005), 3469-3482; DOI  10.1099/mic.0.28326-0
© 2005 Society for General Microbiology

The putative lytic transglycosylase VirB1 from Brucella suis interacts with the type IV secretion system core components VirB8, VirB9 and VirB11

Christoph Höppner1, Anna Carle1, Durga Sivanesan2, Sabine Hoeppner3 and Christian Baron1,2

1 Ludwig-Maximilians-Universität, Department Biologie I, Bereich Mikrobiologie, Maria-Ward-Str. 1a, D-80638 München, Germany
2 McMaster University, Department of Biology, 1280 Main St West, Hamilton, ON, Canada LS8 4K1
3 Ludwig-Maximilians-Universität, Gene Center, Feodor-Lynen Str. 25, D-81377 München, Germany

Correspondence
Christian Baron
baronc{at}mcmaster.ca

VirB1-like proteins are believed to act as lytic transglycosylases, which facilitate the assembly of type IV secretion systems via localized lysis of the peptidoglycan. This paper presents the biochemical analysis of interactions of purified Brucella suis VirB1 with core components of the type IV secretion system. Genes encoding VirB1, VirB8, VirB9, VirB10 and VirB11 were cloned into expression vectors; the affinity-tagged proteins were purified from Escherichia coli, and analyses by gel filtration chromatography showed that they form monomers or homo-multimers. Analysis of protein–protein interactions by affinity precipitation revealed that VirB1 bound to VirB9 and VirB11. The results of bicistron expression experiments followed by gel filtration further supported the VirB1–VirB9 interaction. Peptide array mapping identified regions of VirB1 that interact with VirB8, VirB9 and VirB11 and underscored the importance of the C-terminus, especially for the VirB1–VirB9 interaction. The binding sites were localized on a structure model of VirB1, suggesting that different portions of VirB1 may interact with other VirB proteins during assembly of the type IV secretion machinery.

Abbreviations: S2B, StrepII buffer; T4SS, type IV secretion system(s)




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