Host-parasite interaction in human onchocerciasis: identification and sequence analysis of a novel human calgranulin.
A novel S100 ca2+-binding protein, termed calgranulin-related protein (CGRP), was purified to homogeneity from extracts of adult Onchocerca volvulus, a human tissue-dwelling parasite. Its complete amino acid sequence was determined using microanalytical techniques. The primary structure of CGRP consists of 91 residues and displays identity with the recently reported partial sequence of an S100 protein present in human neutrophils. The human origin of CGRP is supported by the occurrence in O. volvulus extracts of additional human neutrophil proteins, including migration inhibitory factor-related protein 8 and defensins. The results suggest that these proteins interact with the worm surface following their release by activated neutrophils in the course of inflammatory reactions caused by O. volvulus infection.
Marti
T
T
Department of Molecular Biology, Bernhard Nocht Insitute for Tropical Medicine, Hamburg, Germany.
Erttmann
K D
KD
Gallin
M Y
MY
D000595:Amino Acid Sequence; D000818:Animals; D001798:Blood Proteins / Q000737:chemistry / Q000378:metabolism; D006790:Host-Parasite Interactions; D006801:Humans; D006868:Hydrolysis; D039841:Leukocyte L1 Antigen Complex; D008969:Molecular Sequence Data; D019006:Neural Cell Adhesion Molecules / Q000737:chemistry / Q000378:metabolism*; D009504:Neutrophils / Q000378:metabolism; D017181:Onchocerca volvulus; D009855:Onchocerciasis / Q000378:metabolism / Q000469:parasitology*; D017386:Sequence Homology, Amino Acid
D001798:Blood Proteins; D039841:Leukocyte L1 Antigen Complex; D019006:Neural Cell Adhesion Molecules