Abstract:
:Previous studies with monoclonal antibodies of the antigenic structure of bovine leukemia virus (BLV) envelope glycoprotein (gp51) have identified three epitopes (F, G, H) directly involved in the infectivity of BLV, F, G, and H lost their reactivity with the respective monoclonal antibodies after treatment with a reducing agent, indicating that these epitopes were conformational. Sequence comparisons between BLV mutants and differential reactivities of urokinase or proteinase K gp51 fragments with monoclonal antibodies indicated that the NH2 moiety of the env protein harbored the three architectural determinants F, G, and H. ELISA tests demonstrated that anti-F, -G, and -H monoclonal antibodies were maximally reactive toward intact virions whereas they showed much poorer affinities for their respective epitopes when presented on a purified protein. Accordingly, an efficient vaccine against BLV infection will include at least the identified gp51 region presented in its native architectural configuration.
journal_name
Virologyjournal_title
Virologyauthors
Portetelle D,Couez D,Bruck C,Kettmann R,Mammerickx M,Van der Maaten M,Brasseur R,Burny Adoi
10.1016/0042-6822(89)90037-8subject
Has Abstractpub_date
1989-03-01 00:00:00pages
27-33issue
1eissn
0042-6822issn
1096-0341journal_volume
169pub_type
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