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Clinical and Diagnostic Laboratory Immunology, May 1999, p. 377-382, Vol. 6, No. 3
1071-412X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Helicobacter pylori Heat Shock Protein A: Serologic Responses and Genetic Diversity

Enders K. W. Ng,1,2,* Stuart A. Thompson,1 Guillermo I. Pérez-Pérez,1 Imad Kansau,3 Arie van der Ende,4 Agnès Labigne,3 Joseph J. Y. Sung,5 S. C. Sydney Chung,2 and Martin J. Blaser1,6

Division of Infectious Diseases, Department of Medicine, Vanderbilt University School of Medicine,1 and Veteran Affairs Medical Center, Nashville, Tennessee6; Unité de Pathogénie Bactérienne des Muqueuses, Institut Pasteur, Paris, France3; Department of Medical Microbiology, Academic Medical Center, Amsterdam, The Netherlands4; and Department of Medicine and Therapeutics5 and Department of Surgery,2 Prince of Wales Hospital, The Chinese University of Hong Kong, Hong Kong

Received 24 July 1998/Returned for modification 7 October 1998/Accepted 8 February 1999

Helicobacter pylori synthesizes an unusual GroES homolog, heat shock protein A (HspA). The present study was aimed at an assessment of the serological response to HspA in a group of Chinese patients with defined gastroduodenal pathologies and determination of whether diversity is present in the nucleotide sequences encoding HspA in isolates from these patients. Serum samples collected from 154 patients who had an upper gastrointestinal pathology and the presence of H. pylori defined by biopsy were tested for an immunoglobulin G (IgG) serologic response to H. pylori HspA by an enzyme linked immunosorbant assay. HspA-encoding nucleotide sequences in H. pylori isolates from 14 patients (7 seropositive and 7 seronegative for HspA) were analyzed by PCR and direct sequencing of the PCR products. The sequencing results were compared to those of 48 isolates from other parts of the world. Of the 154 known H. pylori-positive patients, 54 (35.1%) were seropositive for HspA. The A domain (GroES homology) of HspA was highly conserved in the 14 isolates tested. Although the B domain (metal-binding site unique to H. pylori) resembled that in the known major variant, particular amino acid substitutions allowed definition of an HspA variant associated with isolates from East Asia. There were no associations between patient characteristics and HspA seropositivity or amino acid sequences. We confirmed in this study that the clinical outcomes of H. pylori infection are not related to HspA antigenicity or to sequence variation. However, B-domain sequence variation may be a marker for the study of the genetic diversity of H. pylori strains of different geographic origins.

* Corresponding author. Mailing address: Department of Surgery, Prince of Wales Hospital, Shatin, N.T., Hong Kong. Fax: (852) 26350075. E-mail: endersng{at}netvigator.com.

Clinical and Diagnostic Laboratory Immunology, May 1999, p. 377-382, Vol. 6, No. 3
1071-412X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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