Leishmania mexicana: binding of promastigotes to type I collagen.
During leishmania infection, parasites are inoculated to the human host through the bite of a sandfly vector into the dermis, where they first interact with tissue components, cells and extracellular matrix molecules. Since collagen is the most abundant component of the skin matrix, we investigated whether there is a specific interaction of Leishmania mexicana promastigotes with this host component. Promastigotes were able to attach to collagen fibrils and move through the matrix of mouse skin sections and to penetrate easily into a type I collagen gel. Denatured type I collagen coated beads (Cytodex 3) readily bound to the parasite surface. The interaction of promastigotes with type I collagen was dose dependent and saturable and was competitively and specifically inhibited with increasing concentrations of gelatin. Biotin-labeled parasite surface molecules were able to associate with both denatured collagen from microcarriers and native type I collagen from bovine kidney. It is suggested that the presence of parasite cell membrane receptors to collagen may confer a specific tropism for the skin, where collagen is the most abundant component of the matrix.
Lira
R
R
Department of Experimental Pathology, Center for Research and Advanced Studies, National Polytechnical Institute, Mexico, DF.
Rosales-Encina
J L
JL
Argüello
C
C
D000818:Animals; D001710:Biotin; D003094:Collagen / Q000378:metabolism*; D005629:Frozen Sections; D006801:Humans; D007894:Leishmania mexicana / Q000378:metabolism* / Q000648:ultrastructure; D016774:Leishmaniasis, Diffuse Cutaneous / Q000469:parasitology*; D051379:Mice; D008854:Microscopy, Electron; D008855:Microscopy, Electron, Scanning; D008863:Microspheres; D012867:Skin / Q000737:chemistry / Q000378:metabolism / Q000469:parasitology* / Q000648:ultrastructure
D001710:Biotin; D003094:Collagen