Bovine papillomavirus type 1: from clathrin to caveolin.
Viruses may infect cells through clathrin-dependent, caveolin-dependent, or clathrin- and caveolin-independent endocytosis. Bovine papillomavirus type 1 (BPV1) entry into cells has been shown to occur by clathrin-dependent endocytosis, a pathway that involves the formation of clathrin-coated pits and fusion to early endosomes. Recently, it has been demonstrated that the closely related JC virus can enter cells in clathrin-coated vesicles and subsequently traffic to caveolae, the organelle where vesicles of the caveolin-dependent pathway deliver their cargo. In this study, we use immunofluorescence staining of BPV1 pseudovirions to show that BPV1 overlaps with the endosome marker EEA1 early during infection and later colocalizes with caveolin-1. We provide evidence through the colocalization of BPV1 with transferrin and cholera toxin B that BPVl trafficking may not be restricted to the clathrin-dependent pathway. Disrupting the entry of caveolar vesicles did not affect BPV1 infection; however, we show that blocking the caveolar pathway postentry results in a loss of BPV1 infection. These data indicate that BPV1 may enter by clathrin-mediated endocytosis and then utilize the caveolar pathway for infection, a pattern of trafficking that may explain the slow kinetics of BPV1 infection.
Laniosz
Valerie
V
Department of Microbiology and Immunology, H. M. Bligh Cancer Research Laboratory, Rosalind Franklin University of Medicine and Science, North Chicago, IL 60064, USA.
Holthusen
Kirsten A
KA
Meneses
Patricio I
PI
D015153:Blotting, Western; D052688:Bovine papillomavirus 1 / Q000502:physiology*; D022461:Caveolins / Q000378:metabolism*; D002772:Cholera Toxin / Q000378:metabolism; D002966:Clathrin / Q000378:metabolism*; D004705:Endocytosis / Q000502:physiology*; D005455:Fluorescent Antibody Technique; D014168:Transferrin / Q000378:metabolism; D053586:Virus Internalization
D022461:Caveolins; D002966:Clathrin; D014168:Transferrin; D002772:Cholera Toxin