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Malaria Sporozoites Release Circumsporozoite Protein from Their Apical End and Translocate It along Their Surface
Author(s) -
STEWART MICHAEL J.,
VANDERBERG JEROME P.
Publication year - 1991
Publication title -
the journal of protozoology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.067
H-Index - 77
eISSN - 1550-7408
pISSN - 0022-3921
DOI - 10.1111/j.1550-7408.1991.tb01379.x
Subject(s) - circumsporozoite protein , microbiology and biotechnology , malaria , virology , biology , immunology , plasmodium falciparum
Plasmodium sporozoites, the causative agents of malaria, release circumsporozoite (CS) protein into medium when under conditions simulating those that the parasites encounter in the bloodstream of the vertebrate host. CS protein of the rodent parasite, Plasmodium berghei , is released as the lower molecular weight form, Pb44. This release is substratum‐ and antibody‐independent. Previous studies show that CS protein is released at the trailing, posterior end of motile sporozoites. Video and electron microscopic studies now demonstrate that CS protein is released at the apical end of cytochalasin b‐immobilized sporozoites. We propose that CS protein released from the apical end, the leading end of gliding sporozoites, adheres to the sporozoite surface and is translocated posteriorly by a cytochalasin‐sensitive and apparently actin‐mediated surface motor, which drives gliding motility. This model explains the mechanism of both the circumsporozoite precipitation (CSP) reaction and formation of the CS protein trail by gliding sporozoites.