
Sequence and Antigenic Variability of the Helicobacter mustelae Surface Ring Protein Hsr
Author(s) -
Natasha T. Forester,
John S. Lumsden,
Tadhg Ó'Cróinín,
Paul W. O’Toole
Publication year - 2001
Publication title -
infection and immunity
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.508
H-Index - 220
eISSN - 1070-6313
pISSN - 0019-9567
DOI - 10.1128/iai.69.5.3447-3450.2001
Subject(s) - biology , epitope , bacterial adhesin , genetics , gene , peptide sequence , mutant , sequence analysis , sequence alignment , helicobacter , antigen , pathogen , virulence , helicobacter pylori
We have identified an array of more than 500 repetitive sequences flanking the hsr gene, which encodes the major surface protein of the ferret pathogen Helicobacter mustelae. The repeats show identity exclusively to the amino-terminal half of Hsr. Analysis of Hsr from three strains indicated variability of exposed epitopes. Characterization of an hsr mutant showed that Hsr is not an adhesin.