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Microbiology 143 (1997), 1805-1813; DOI  10.1099/00221287-143-6-1805
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VlpA of Vibrio cholerae O1: the first bacterial member of the {alpha}2-microglobulin lipocalin superfamily

Andrew Barker{dagger} and Paul A. Manning

Microbial Pathogenesis Unit, Department of Microbiology and Immunology, University of Adelaide, Adelaide, South Australia 5005, Australia

Author for correspondence: Paul A. Manning. Tel: + 61 8 83035974. Fax: +61 8 83034362. e-mail: pmanning@microb.adelaide.edu.au

ABSTRACT

We have identified a gene, vlpA, which is closely linked to the mfrA,B locus associated with mannose-fucose-resistant haemagglutination. VlpA is an outer-membrane protein which can be labelled with [3H]palmitate and whose processing is globomycin-sensitive, suggesting that it is a lipoprotein. Homology searches revealed that VlpA belongs to the group of lipocalins of the {alpha}2-microglobulin superfamily which function as small hydrophobic molecule transporters, and is the first identified bacterial member of this group. Multiple copies of this gene are present in Vibrio cholerae O1 and O139 and Southern hybridization reveals a biotype-specific pattern of fragment sizes. Construction of strains capable of hyperproducing VlpA suggested that it is able to bind haemin with low affinity but this may be due to a simple hydrophobic interaction. Attempts to construct specific mutants in vlpA have been unsuccessful, presumably because of the multiple copies of vlpA genes and their linkage to the VCR element.


Keywords: Vibrio cholerae, lipoprotein, {alpha}2-microglobulin, lipocalin, haemin binding

{dagger} Current address: Institut für Genetik der Universität zu Köln, Weyertal 121, D-50931 Köln, Germany.




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