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Infect. Immun., 02 1996, 460-465, Vol 64, No. 2
JW Marsh, D Sun and RK Taylor
Vibrio cholerae O1 expresses a variety of cell surface factors which
mediate bacterial adherence and colonization at the intestinal epithelium.
The mannose-sensitive hemagglutinin (MSHA), a type IV pilus, is a potential
attachment factor of the V. cholerae El Tor biotype. We describe a TnphoA
mutant that is defective in its ability to hemagglutinate mouse
erythrocytes. The TnphoA insertion maps to a recently identified genetic
locus that encodes products that are predicted to be essential for assembly
and export of the MSHA pilus. Insertional disruption at this locus in a
mshA-phoA reporter strain provides evidence for a role of this locus in the
latter stages of pilus assembly and/or export. These constructs have
provided physical markers by which we have established close physical
linkage of this secretion locus to a set of genes that includes the mshA
structural gene. Sequence analysis of the intervening region between these
two loci has revealed the presence of an open reading frame with homology
to pilus biogenesis genes of several gram-negative bacteria. This genetic
organization suggests an entire operon encoding the MSHA pilus and the
components necessary for its assembly and secretion to the bacterial cell
surface. The nomenclature of the MSHA structural and secretory locus has
been redefined accordingly.
Copyright © 1996, American Society for Microbiology
Physical linkage of the Vibrio cholerae mannose-sensitive hemagglutinin secretory and structural subunit gene loci: identification of the mshG coding sequence
Department of Microbiology, Dartmouth Medical School, Hanover, New Hampshire 03755, USA.
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