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Infection and Immunity, November 2001, p. 6846-6852, Vol. 69, No. 11
Department of
Microbiology,1 Second Department of
Internal Medicine,2 and First Department
of Biochemistry,3 Oita Medical University,
Oita, Japan
Received 3 May 2001/Returned for modification 10 July 2001/Accepted 7 August 2001
We purified a 29-kDa Helicobacter pylori outer
membrane protein (Omp29 protein) and cloned the gene encoding the
protein from H. pylori strain ATCC 43504. The Omp29 gene
corresponded to the reported JHP73 and the HP78-79 genes of H.
pylori strains. A corresponding nucleotide fragment was
detected in all 150 tested H. pylori clinical isolates
by PCR or Southern blotting. The amplified Omp29-corresponding fragments were categorized into a ca. 770-bp-long group and a larger-fragment group. Sequence analysis indicated that the larger fragments were likely synthesized from the 770-bp fragments by insertion of an irrelevant fragment via 17-bp-long repeat sequences. Immunoblot analysis implies that the ca. 770-bp fragment is responsible for the protein homologous to Omp29, whereas the larger fragments are
not responsible for those proteins or encoding antigenically distinct
proteins. We postulate that the H. pylori outer membrane protein Omp29 can alter its antigenicity through gene modifications mediated by nucleotide transfer.
0019-9567/01/$04.00+0 DOI: 10.1128/IAI.69.11.6846-6852.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
Comparison of Genomic Structures and Antigenic Reactivities of
Orthologous 29-Kilodalton Outer Membrane Proteins of
Helicobacter pylori
*
Corresponding author. Mailing address: Department of
Microbiology, Oita Medical University, Hasama-machi, Oita 879-5593, Japan. Phone: 81-97-586-5710. Fax: 81-97-586-5719. E-mail:
a24zono{at}oita-med.ac.jp.
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