Host specificity in blood feeding parasites: a defining contribution by haemoglobin-degrading enzymes?

被引：18

作者：

Brinkworth, RI

Harrop, SA

Prociv, P

Brindley, PJ ^{[1
]}

机构：

[1] Tulane Univ, Sch Publ Hlth & Trop Med, Dept Trop Med, New Orleans, LA 70112 USA

[2] Univ Queensland, Ctr Drug Design & Dev, Brisbane, Qld, Australia

[3] Univ Queensland, Dept Microbiol & Parasitol, Brisbane, Qld, Australia

[4] Univ Queensland, Australian Ctr Int & Trop Hlth & Nutr, Brisbane, Qld, Australia

[5] Queensland Inst Med Res, Mol Parasitol Unit, Brisbane, Qld 4006, Australia

来源：

INTERNATIONAL JOURNAL FOR PARASITOLOGY | 2000年 / 30卷 / 06期

基金：

英国医学研究理事会;

关键词：

cathepsin D; haematophagy; hookworm; host specificity; protease;

D O I：

10.1016/S0020-7519(00)00045-X

中图分类号：

R38 [医学寄生虫学]; Q [生物科学];

学科分类号：

07 ; 0710 ; 09 ; 100103 ;

摘要：

A hypothesis is presented that proposes that the compatibility between species-specific variants of haemoglobin-degrading proteases of blood-feeding parasites (e.g. hookworms, schistosomes, malarial parasites, etc.), and their natural substrates, i.e. haemoglobins from diverse species of mammals, has influenced to evolution of the host range of these parasites. Support for the hypothesis was drawn from molecular modelling studies of the three dimensional structure of an aspartic protease, Acasp, from the canine hookworm Ancylostoma caninum, and models of canine and human haemoglobins docked with the active site of Acasp. The molecular modelling suggested that Acasp, from a canine-specific hookworm, would have a higher substrate affinity for canine haemoglobin than for human haemoglobin. (C) 2000 Australian Society for Parasitology Inc. Published by Elsevier Science Ltd. All rights reserved.

引用

页码：785 / 790

页数：6

共 33 条

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