NISCAIR Online Periodicals Repository

NISCAIR ONLINE PERIODICALS REPOSITORY (NOPR)  >
NISCAIR PUBLICATIONS >
Research Journals >
Indian Journal of Biochemistry and Biophysics (IJBB) >
IJBB Vol.44 [2007] >
IJBB Vol.44(6) [December 2007] >


Title: Biochemical and immunological characterization of E. coli expressed 42 kDa fragment of Plasmodium vivax and P. cynomolgi bastianelli merozoite surface protein-1
Authors: Kaushal, Deep C
Kaushal, Nuzhat A
Narula, Atul
Kumar, Niraj
Puri, S K
Dutta, Shitij
Lanar, David E
Keywords: Plasmodium vivax
Plasmodium cynomolgi
Malaria
Vaccine
Merozoite surface protein-1
Merozoite
Rhesus monkey
Issue Date: Dec-2007
Publisher: CSIR
Abstract: Plasmodium vivax is one of the most widely distributed human malaria parasites and due to drug-resistant strains, its incidence and prevalence has increased, thus an effective vaccine against the parasites is urgently needed. One of the major constraints in developing P. vivax vaccine is the lack of suitable in vivo models for testing the protective efficacy of the vaccine. P. vivax and P. cynomolgi bastianelli are the two closely related malaria parasites and share a similar clinical course of infection in their respective hosts. The merozoite surface protein-1 (MSP-1) of these parasites has found to be protective in a wide range of host-parasite systems. P. vivax MSP-1 is synthesized as 200 kDa polypeptide and processed just prior to merozoite release from the erythrocytes into smaller fragments. The C- terminal 42 kDa cleavage product of MSP-1 (MSP-1₄₂) is present on the surface of merozoites and a major candidate for blood stage malaria vaccine. In the present study, we have biochemically and immunologically characterized the soluble and refolded 42 kDa fragment of MSP-1 of P. vivax (PvMSP-1₄₂) and P. cynomolgi B (PcMSP-1₄₂). SDS-PAGE analysis showed that both soluble and refolded E. coli expressed P. vivax and P. cynomolgi B MSP-1₄₂ proteins were homogenous in nature. The soluble and refolded MSP-1₄₂ antigens of both parasites showed high reactivity with protective monkey sera and conformation-specific monoclonal antibodies against P. cynomolgi B and P. vivax MSP-1₄₂ antigens. Immunization of BALB/c mice with these antigens resulted in the production of high titres of cross-reactive antibodies primarily against the conformational epitopes of MSP-1₄₂ protein. The immune sera from rhesus monkeys, immunized with soluble and refolded MSP-142 antigens of both parasites also showed high titered cross-reactive antibodies against MSP-1₄₂ conformational epitopes. These results suggested that the soluble and refolded forms of E. coli expressed P. vivax MSP-1₄₂ antigens were highly immunogenic and thus a viable candidate for vaccine studies.
Page(s): 429-436
ISSN: 0301-1208
Source:IJBB Vol.44(6) [December 2007]

Files in This Item:

File Description SizeFormat
IJBB 44(6) (2007) 429-436.pdf311.89 kBAdobe PDFView/Open
 Current Page Visits: 651 
Recommend this item

 

National Knowledge Resources Consortium |  NISCAIR Website |  Contact us |  Feedback

Disclaimer: NISCAIR assumes no responsibility for the statements and opinions advanced by contributors. The editorial staff in its work of examining papers received for publication is helped, in an honorary capacity, by many distinguished engineers and scientists.

CC License Except where otherwise noted, the Articles on this site are licensed under Creative Commons License: CC Attribution-Noncommercial-No Derivative Works 2.5 India

Copyright © 2012 The Council of Scientific and Industrial Research, New Delhi. All rights reserved.

Powered by DSpace Copyright © 2002-2007 MIT and Hewlett-Packard | Compliant to OAI-PMH V 2.0

Home Page Total Visits: 512907 since 06-Feb-2009  Last updated on 21-Apr-2014Webmaster: nopr@niscair.res.in