MHC Class I Molecules Are Enriched in Caveolae but Do Not Enter With Simian Virus 40

J Gen Virol. 1998 Jun;79 ( Pt 6):1469-77. doi: 10.1099/0022-1317-79-6-1469.

Abstract

Simian virus 40 (SV40) binds to MHC class I molecules anywhere on the cell surface and then enters through caveolae. The fate of class I molecules after SV40 binding is not known. Sensitivity of 125I-surface-labelled class I molecules to papain cleavage was used to distinguish internalized class I molecules from class I molecules remaining at the cell surface. Whereas the caveolae-enriched membrane microdomain was found to also be enriched for class I molecules, no internalized papain-resistant 125I-surface-labelled class I molecules could be detected at any time in either control cells or in cells preadsorbed with saturating amounts of SV40. Instead, 125I-surface-labelled class I molecules, as well as preadsorbed 125I-labelled anti-class I antibodies, accumulated in the medium, coincident with the turnover of class I molecules at the cell surface. The class I heavy chains that accumulated in the medium were truncated and their release was specifically prevented by the metalloprotease inhibitor 1,10-phenanthroline. Thus, whereas class I molecules mediate SV40 binding, they do not appear to mediate SV40 entry.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Caveolin 1
  • Caveolins*
  • Cell Line
  • Cell Membrane / metabolism
  • Chlorocebus aethiops
  • Histocompatibility Antigens Class I / metabolism*
  • Humans
  • Membrane Proteins / metabolism
  • Simian virus 40 / metabolism*
  • Simian virus 40 / physiology

Substances

  • Caveolin 1
  • Caveolins
  • Histocompatibility Antigens Class I
  • Membrane Proteins