These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Membrane-bound antiviral antibodies as receptors for Sendai virions in receptor-depleted erythrocytes.
    Author: Nussbaum O, Zakai N, Loyter A.
    Journal: Virology; 1984 Oct 30; 138(2):185-97. PubMed ID: 6093364.
    Abstract:
    Anti-Sendai virus antibodies were covalently coupled to neuraminidase-treated human erythrocytes by the use of the bifunctional crosslinking reagents, N-succinimidyl-3-(2-pyridyldithio)propionate or succinimidyl-4-(p-maleimidophenyl)butyrate. Neuraminidase-treated erythrocytes bearing antibodies were able to bind Sendai virus particles, while treated erythrocytes lacking the antibodies failed to do so. Virus particles attached to erythrocyte membranes via the antibodies were able to cause hemolysis (virus-cell fusion) and promoted cell-cell fusion. Similar results were obtained when the antibodies were coupled to cat erythrocytes which lack receptors for Sendai virus particles. Reconstituted Sendai virus envelopes, similar to intact virus particles, were able to hemolyze and to induce fusion of neuraminidase-treated antibody-bearing erythrocytes. However, reconstituted envelopes containing inactive HN (hemagglutinin-neuraminidase) but active F (fusion) glycoproteins, despite attachment to antibody-bearing erythrocytes, failed to hemolyze or to induce cell-to-cell fusion. Fusion could be restored by insertion of an active HN glycoprotein into the membranes of the reconstituted envelopes. These results suggest that the HN glycoprotein, besides being the viral attachment protein, also participates in the membrane fusion process.
    [Abstract] [Full Text] [Related] [New Search]