VlpA of Vibrio cholerae O1: the first bacterial member of the α2-microglobulin lipocalin superfamily
- 1 June 1997
- journal article
- Published by Microbiology Society in Microbiology
- Vol. 143 (6) , 1805-1813
- https://doi.org/10.1099/00221287-143-6-1805
Abstract
We have identified a gene,vlpA,which is closely linked to themfrA,Blocus 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 α2-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 inVibrio choleraeO1 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 invlpAhave been unsuccessful, presumably because of the multiple copies ofvlpAgenes and their linkage to the VCR element.Keywords
This publication has 44 references indexed in Scilit:
- CLUSTAL: a package for performing multiple sequence alignment on a microcomputerPublished by Elsevier ,2003
- The toxin-co-regulated pilus of Vibrio cholerae 01: a model for type 4 pilus biogenesis?Trends in Microbiology, 1994
- Cloning and characterization of the Vibrio cholerae genes encoding the utilization of iron from haemin and haemoglobinMolecular Microbiology, 1993
- TCP pilus biosynthesis inVibrio choleraO1: gene sequence of tcpC encoding an outer membrane lipoproteinFEMS Microbiology Letters, 1992
- Molecular cloning, partial purification, and characterization of a haemin‐binding lipoprotein from Haemophilus influenzae type bMolecular Microbiology, 1991
- Structural homology of human complement component C8γ and plasma protein HC: Identity of the cysteine bond patternBiochemical and Biophysical Research Communications, 1987
- Molecular structure of the bilin binding protein (BBP) from Pieris brassicae after refinement at 2.0 Å resolutionJournal of Molecular Biology, 1987
- Sequence analysis, cellular localization, and expression of a neuroretina adhesion and cell survival moleculeCell, 1987
- One fold among manyNature, 1987
- A chick neural retina adhesion and survival molecule is a retinol-binding protein.The Journal of cell biology, 1986