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ARS Home » Research » Publications at this Location » Publication #47483
Title: CHARACTERIZATION OF BIOLOGICALLY ACTIVE OVINE LENTIVIRUS ENVELOPE GLYCOPROTEIN EXPRESSED IN ESCHERICHIA COLI CELL AND BACULOVIRUS SYSTEMS

Author
item KWANG JIMMY - 5438-01-35
item KIM HYUN SOO - 5438-01-35
item ROSATI SERGIO - UNIV. OF TURIN, ITALY
item Lehmkuhl, Howard

Submitted to: Veterinary Immunology and Immunopathology
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 4/6/1994
Publication Date: N/A
Citation: N/A

Interpretive Summary: Ovine progressive pneumonia (OPP) is a predominant clinical syndrome associated with chronic respiratory disease of sheep. The causative virus (OPP virus) is similar to the human AIDS virus, but does not cross infect humans. In this study, we used molecular biologic techniques to produce outer membrane proteins in E. coli and insect cell systems. The purified proteins were injected into guinea pigs and sheep to produce antibodies against these proteins. Antibodies produced in E. coli and insect cell systems were able to block virus infectivity. We were able to identify the portion of the viral outer membrane that when combined with antibodies prevents the virus' ability to infect cells. This portion of the outer membrane of OPP virus differs from that of the human AIDS virus. Also, in comparing the antibodies to E. coli and insect cell produced viral proteins, the same neutralization activities were observed. This means that both systems produced proteins that may be of equal value in producing a vaccine to prevent OPP.

Technical Abstract: The ovine lentivirus (OLV) envelope subunits NH2- and COOH-terminals of gp70 and NH2-terminal of gp40 were expressed in Escherichia coli cell. The entire gp70 envelope protein was also expressed in insect cells by the recombinant baculovirus. Guinea pigs were immunized with each bacterially expressed recombinant protein and a serum neutralization assay was used to determine their capacity to neutralize OLV. These results showed that the major neutralization epitopes are located in the NH2-terminal half of the gp70. The baculovirus expressed gp70 was found on the surface of insect cells and was biologically active. Virus neutralization activity was also produced in sheep immunized with the recombinant protein.