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  • 1
    Publication Date: 1986-07-11
    Description: Mammalian cell lines have been engineered to produce a secreted form of the AIDS retrovirus envelope glycoprotein. The recombinant protein has been isolated from growth-conditioned culture media and used to immunize animals. Antibodies directed against the recombinant molecule were found to react with the envelope glycoprotein produced in virus-infected cells. Furthermore, these antibodies were able to directly inactivate the AIDS retrovirus in a neutralization assay in vitro. The expression system reported here should provide sufficient quantities of the AIDS retrovirus envelope protein for biological and vaccination studies.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lasky, L A -- Groopman, J E -- Fennie, C W -- Benz, P M -- Capon, D J -- Dowbenko, D J -- Nakamura, G R -- Nunes, W M -- Renz, M E -- Berman, P W -- HL 33774-01/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1986 Jul 11;233(4760):209-12.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3014647" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/*immunology ; Animals ; Antibodies, Viral/*immunology ; Antigens, Viral/biosynthesis/*immunology ; Cricetinae ; Deltaretrovirus/*immunology ; Guinea Pigs ; HIV Antibodies ; HIV Antigens ; Humans ; Immune Sera/immunology ; Male ; Neutralization Tests ; Rabbits ; Recombinant Proteins/biosynthesis/immunology ; Viral Envelope Proteins/biosynthesis/*immunology ; Viral Vaccines/immunology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
    ISSN: 0006-3525
    Keywords: structure-based design ; Vascular Cell Adhesion Molecule ; α4β1 ; integrins ; epitope transfer ; peptides ; receptor ; antagonists ; nmr spectroscopy ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Results from protein mutagenesis and x-ray crystallographic studies of the multidomain protein Vascular Cell Adhesion Molecule (VCAM) were used to design cyclic octapeptides that retain the critical structural and binding elements of the epitope of VCAM in the interaction with the integrin α4β1 (VLA-4). Changes in the activities of peptide analogues correlated with the relative activities of protein mutants of VCAM, and predicted the properties of two new mutants that bound α4β1 with improved affinity vs wild type protein. The nmr structures of two peptides revealed a high degree of similarity to the structure of the VCAM binding epitope. These results demonstrate that a compact binding epitope identified via protein structure-function studies may be transferred to a synthetically accessible small peptide with the key structure-activity relationships intact. © 1998 John Wiley & Sons, Inc. Biopoly 47: 265-275, 1998
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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