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Infection and Immunity, March 2002, p. 1581-1590, Vol. 70, No. 3
0019-9567/02/$04.00+0     DOI: 10.1128/IAI.70.3.1581-1590.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Monoclonal Antibody against the Plasmodium falciparum Chitinase, PfCHT1, Recognizes a Malaria Transmission-Blocking Epitope in Plasmodium gallinaceum Ookinetes Unrelated to the Chitinase PgCHT1

Rebecca C. Langer,1,2,{dagger} Fengwu Li,1,2 Vsevolod Popov,1,2 Alexander Kurosky,3 and Joseph M. Vinetz1,2*

World Health Organization Collaborating Center for Tropical Diseases,1 Department of Pathology,2 Department of Human Biological Chemistry and Genetics, University of Texas Medical Branch, Galveston, Texas 775553

Received 29 October 2001/ Returned for modification 22 November 2001/ Accepted 3 December 2001

To initiate invasion of the mosquito midgut, Plasmodium ookinetes secrete chitinases that are necessary to cross the chitin-containing peritrophic matrix en route to invading the epithelial cell surface. To investigate chitinases as potential immunological targets of blocking malaria parasite transmission to mosquitoes, a monoclonal antibody (MAb) was identified that neutralized the enzymatic activity of the sole chitinase of Plasmodium falciparum, PfCHT1, identified to date. This MAb, designated 1C3, previously shown to react with an apical structure of P. falciparum ookinetes, also reacts with a discrete apical structure of P. gallinaceum ookinetes. In membrane feeding assays, MAb 1C3 markedly inhibited P. gallinaceum oocyst development in mosquito midguts. MAb 1C3 affinity isolated an ~210-kDa antigen which, under reducing conditions, became a 35-kDa antigen. This isolated 35-kDa protein cross-reacted with an antiserum raised against a synthetic peptide derived from the P. gallinaceum chitinase active site, PgCHT1, even though MAb 1C3 did not recognize native or recombinant PgCHT1 on Western blot. Therefore, this affinity-purified 35-kDa antigen appears similar to a previously identified protein, PgCHT2, a putative second chitinase of P. gallinaceum. Epitope mapping indicated MAb 1C3 recognized a region of PfCHT1 that diverges from a homologous amino acid sequence conserved within sequenced chitinases of P. berghei, P. yoelii, and P. gallinaceum (PgCHT1). A synthetic peptide derived from the mapped 1C3 epitope may be useful as a component of a subunit transmission-blocking vaccine.

* Corresponding author. Mailing address: WHO Collaborating Center for Tropical Disease, Keiller 2.138, University of Texas Medical Branch, Galveston, TX 77555-0609. Phone: (409) 747-2962. Fax: (409) 747-2437. E-mail: jovinetz{at}utmb.edu.

{dagger} Present address: University of Texas-Houston School of Public Health, Houston, TX 77030.

Infection and Immunity, March 2002, p. 1581-1590, Vol. 70, No. 3
0019-9567/02/$04.00+0     DOI: 10.1128/IAI.70.3.1581-1590.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Li, F., Templeton, T. J., Popov, V., Comer, J. E., Tsuboi, T., Torii, M., Vinetz, J. M. (2004). Plasmodium Ookinete-secreted Proteins Secreted through a Common Micronemal Pathway Are Targets of Blocking Malaria Transmission. J. Biol. Chem. 279: 26635-26644 [Abstract] [Full Text]  


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