The complete genome sequence of the gastric pathogen Helicobacter pylori View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

1997-08

AUTHORS

Jean-F. Tomb, Owen White, Anthony R. Kerlavage, Rebecca A. Clayton, Granger G. Sutton, Robert D. Fleischmann, Karen A. Ketchum, Hans Peter Klenk, Steven Gill, Brian A. Dougherty, Karen Nelson, John Quackenbush, Lixin Zhou, Ewen F. Kirkness, Scott Peterson, Brendan Loftus, Delwood Richardson, Robert Dodson, Hanif G. Khalak, Anna Glodek, Keith McKenney, Lisa M. Fitzegerald, Norman Lee, Mark D. Adams, Erin K. Hickey, Douglas E. Berg, Jeanine D. Gocayne, Teresa R. Utterback, Jeremy D. Peterson, Jenny M. Kelley, Matthew D. Cotton, Janice M. Weidman, Claire Fujii, Cheryl Bowman, Larry Watthey, Erik Wallin, William S. Hayes, Mark Borodovsky, Peter D. Karp, Hamilton O. Smith, Claire M. Fraser, J. Craig Venter

ABSTRACT

Helicobacter pylori, strain 26695, has a circular genome of 1,667,867 base pairs and 1,590 predicted coding sequences. Sequence analysis indicates that H. pylori has well-developed systems for motility, for scavenging iron, and for DNA restriction and modification. Many putative adhesins, lipoproteins and other outer membrane proteins were identified, underscoring the potential complexity of host-pathogen interaction. Based on the large number of sequence-related genes encoding outer membrane proteins and the presence of homopolymeric tracts and dinucleotide repeats in coding sequences, H. pylori, like several other mucosal pathogens, probably uses recombination and slipped-strand mispairing within repeats as mechanisms for antigenic variation and adaptive evolution. Consistent with its restricted niche, H. pylori has a few regulatory networks, and a limited metabolic repertoire and biosynthetic capacity. Its survival in acid conditions depends, in part, on its ability to establish a positive inside-membrane potential in low pH. More... »

PAGES

539-547

References to SciGraph publications

  • 1996. Gene Cloning of a Flagellar Sheath Protein of Helicobacter Pylori in CAMPYLOBACTERS, HELICOBACTERS, AND RELATED ORGANISMS
  • 1996-08. tRNA-dependent asparagine formation in NATURE
  • Journal

    TITLE

    Nature

    ISSUE

    6642

    VOLUME

    388

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/41483

    DOI

    http://dx.doi.org/10.1038/41483

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1043803227

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/9252185


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