Caveolin-1 mediated uptake via langerin restricts HIV-1 infection in human Langerhans cells

Retrovirology. 2014 Dec 31:11:123. doi: 10.1186/s12977-014-0123-7.

Abstract

Background: Human Langerhans cells (LCs) reside in foreskin and vaginal mucosa and are the first immune cells to interact with HIV-1 during sexual transmission. LCs capture HIV-1 through the C-type lectin receptor langerin, which routes the virus into Birbeck granules (BGs), thereby preventing HIV-1 infection. BGs are langerin-positive organelles exclusively present in LCs, however, their origin and function are unknown.

Results: Here, we not only show that langerin and caveolin-1 co-localize at the cell membrane and in vesicles but also that BGs are langerin/caveolin-1-positive vesicles are linked to the lysosomal degradation pathway in LCs. Moreover, inhibition of caveolar endocytosis in primary LCs abrogated HIV-1 sequestering into langerin(+) caveolar structures. Notably, both inhibition of caveolar uptake and silencing of caveolar structure protein caveolin-1 resulted in increased HIV-1 integration and subsequent infection. In contrast, inhibition of clathrin-mediated endocytosis did not affect HIV-1 integration, even though HIV-1 uptake was decreased, suggesting that clathrin-mediated endocytosis is not involved in HIV-1 restriction in LCs.

Conclusions: Thus, our data strongly indicate that BGs belong to the caveolar endocytosis pathway and that caveolin-1 mediated HIV-1 uptake is an intrinsic restriction mechanism present in human LCs that prevents HIV-1 infection. Harnessing this particular internalization pathway has the potential to facilitate strategies to combat HIV-1 transmission.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antigens, CD / metabolism*
  • Caveolin 1 / metabolism*
  • Cytoplasmic Vesicles / virology
  • Endocytosis*
  • HIV-1 / physiology*
  • Humans
  • Langerhans Cells / virology*
  • Lectins, C-Type / metabolism*
  • Mannose-Binding Lectins / metabolism*
  • Virus Internalization*

Substances

  • Antigens, CD
  • CD207 protein, human
  • Caveolin 1
  • Lectins, C-Type
  • Mannose-Binding Lectins