Premium
Toward the elucidation of the mechanism of attachment and entry of malaria sporozoites into cells: Synthetic polypeptides from the circumsporozoite protein of Plasmodium falciparum bind Ca 2+ and interact with model phospholipid membranes
Author(s) -
Verdini Antonio S.,
Chiappinelli Lorella,
Zanobi Antonio
Publication year - 1991
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360310602
Subject(s) - chemistry , plasmodium falciparum , circumsporozoite protein , plasmodium (life cycle) , malaria , mechanism (biology) , microbiology and biotechnology , biophysics , biochemistry , parasite hosting , immunology , biology , world wide web , computer science , philosophy , epistemology
Through the joint use of CD, Fourier transform ir (FTIR), and attenuated total reflectance FTIR we have found that synthetic polypeptide models of the Plasmodium falciparum circumsporozoite (CS) protein repeat domain bind calcium ions in helicogenic environments. Ca 2+ ‐(NANP) n complexes ( n ⩾ 20) interact vectorially with model phospholipid membranes orienting their polypeptide axes preferentially along those of the lipid acyl chains. It is proposed that the P. falciparum CS protein central region, rather than acting as a molecular lure helping the parasite to evade host immune control, plays, as a specific Ca 2+ macroligand, a critical functional role during attachment, invasion, and development of the malaria parasite in the hepatic cell.