The patent badge is an abbreviated version of the USPTO patent document. The patent badge does contain a link to the full patent document.

The patent badge is an abbreviated version of the USPTO patent document. The patent badge covers the following: Patent number, Date patent was issued, Date patent was filed, Title of the patent, Applicant, Inventor, Assignee, Attorney firm, Primary examiner, Assistant examiner, CPCs, and Abstract. The patent badge does contain a link to the full patent document (in Adobe Acrobat format, aka pdf). To download or print any patent click here.

Date of Patent:
Dec. 09, 2003

Filed:

Nov. 10, 2000
Applicant:
Inventors:

George S. N. Hui, Honolulu, HI (US);

Lap-Yin Pang, Kwai Chung, HK;

Walter K. K. Ho, Taipo, HK;

Assignee:

Other;

Attorney:
Primary Examiner:
Int. Cl.
CPC ...
C12P 2/106 ; C12N 1/509 ; A23J 1/00 ; C07K 1/00 ; C07K 1/400 ;
U.S. Cl.
CPC ...
C12P 2/106 ; C12N 1/509 ; A23J 1/00 ; C07K 1/00 ; C07K 1/400 ;
Abstract

We utilized the silkworm ( )/baculovirus system to produce recombinant Major Merozoite Surface Protein 1 (MSP1 ) because of the low cost and potential high yield of this expression system. The MSP1 (3D7 sequence) was cloned into the baculovirus, BmNPV with the melittin signal sequence. The recombinant virus, BmNPV-Sp42 was used to infect silkworms for the expression of MSP1 (Sp42). One recombinant clone expressed high level of Sp42 with an estimated 0.5 mg of antigen produced within a single worm. The Sp42 was recognized by monoclonal and polyclonal antibodies specific for parasite MSP1 in direct binding and competitive binding ELISAs, suggesting that Sp42 possesses antigenic determinants similar to parasite MSP1 . Immunogenicity studies were performed in rabbits. Sp42 induced high titers of antibodies crossreactive with MSP1. Specificity analyses showed that anti-Sp42 antibodies reacted primarily against conserved determinants on MSP1-19. Our results showed that the silkworm expression system can produce recombinant MSP1 that are antigenically and immunogenically comparable to other recombinant MSP1 antigens expressed in other eukaryotic systems. The low cost ad high level of protein expression makes it an attractive alternative for the development of a human malaria vaccine.


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