This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow E-mail this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Winter, L. E.
Right arrow Articles by Barenkamp, S. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Winter, L. E.
Right arrow Articles by Barenkamp, S. J.

 Previous Article  |  Next Article 

Clinical and Vaccine Immunology, July 2009, p. 1040-1046, Vol. 16, No. 7
1071-412X/09/$08.00+0     doi:10.1128/CVI.00090-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Antibodies Specific for the Hia Adhesion Proteins of Nontypeable Haemophilus influenzae Mediate Opsonophagocytic Activity{triangledown}

Linda E. Winter1,2 and Stephen J. Barenkamp1,2*

Department of Pediatrics, Saint Louis University School of Medicine,1 the Pediatric Research Institute, Cardinal Glennon Children's Medical Center, Saint Louis, Missouri 631042

Received 1 March 2009/ Returned for modification 28 March 2009/ Accepted 21 May 2009

The Hia autotransporter proteins are highly immunogenic surface adhesins expressed by nontypeable Haemophilus influenzae (NTHI). The objective of our study was to assess the opsonophagocytic activity of anti-Hia antibodies against homologous and heterologous NTHI. A segment of the hia gene that encodes a surface-exposed portion of the H. influenzae strain 11 Hia protein was cloned into a pGEMEX-2 expression vector. Escherichia coli JM101 was transformed with the resulting pGEMEX-Hia BstEII del recombinant plasmid, and recombinant fusion protein was recovered. An immune serum against recombinant GEMEX-Hia (rGEMEX-Hia)-mediated killing of the homologous NTHI strain 11 at a 1:160 titer and five heterologous Hia-expressing strains at titers of ≥1:40. Immune serum did not mediate killing of two Hia-knockout strains whose hia genes were inactivated but did mediate killing of one knockout strain at a high titer after the strain was transformed with a plasmid containing the hia gene. Immune serum did not mediate killing of HMW1/HMW2-expressing NTHI strains, which do not express the Hia adhesin. However, when two representative HMW1/HMW2-expressing strains were transformed with the plasmid containing the hia gene, they expressed abundant Hia and were susceptible to killing by the immune serum. Immune serum did not mediate killing of HMW1/HMW2-expressing strains transformed with the plasmid without the hia gene. Our results demonstrate that the Hia proteins of NTHI are targets of opsonophagocytic antibodies and that shared epitopes recognized by such antibodies are present on the Hia proteins of unrelated NTHI strains. These data argue for the continued investigation of the Hia proteins as vaccine candidates for the prevention of NTHI disease.

* Corresponding author. Mailing address: St. Louis University School of Medicine, Doisy Research Center, Room 803, 1100 South Grand Boulevard, Saint Louis, MO 63104. Phone: (314) 977-9042. Fax: (314) 268-2712. E-mail: barenksj{at}slu.edu

{triangledown} Published ahead of print on 27 May 2009.

Clinical and Vaccine Immunology, July 2009, p. 1040-1046, Vol. 16, No. 7
1071-412X/09/$08.00+0     doi:10.1128/CVI.00090-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.





Copyright © 2010 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»