Document Type
Article
Publication Date
1996
Publication Title
Infection and Immunity
Department
Geisel School of Medicine
Abstract
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.
Original Citation
Marsh JW, Sun D, Taylor RK. Physical linkage of the Vibrio cholerae mannose-sensitive hemagglutinin secretory and structural subunit gene loci: identification of the mshG coding sequence. Infect Immun. 1996;64(2):460-465. doi:10.1128/IAI.64.2.460-465.1996
Dartmouth Digital Commons Citation
Marsh, Jane W.; Sun, Daxi; and Taylor, Ronald K., "Physical Linkage of the Vibrio Cholerae Mannose-Sensitive Hemagglutinin Secretory and Structural Subunit Gene Loci: Identification of the Mshg Coding Sequence." (1996). Dartmouth Scholarship. 3038.
https://digitalcommons.dartmouth.edu/facoa/3038