Host specificity in blood feeding parasites: a defining contribution by haemoglobin-degrading enzymes?
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.
Brinkworth
R I
RI
Centre for Drug Design & Development, University of Queensland, Brisbane, Australia.
Harrop
S A
SA
Prociv
P
P
Brindley
P J
PJ
D000595:Amino Acid Sequence; D000722:Ancylostoma / Q000201:enzymology* / Q000502:physiology; D000818:Animals; D016282:Aspartic Acid Endopeptidases / Q000737:chemistry / Q000378:metabolism*; D002402:Cathepsin D / Q000737:chemistry / Q000378:metabolism; D004285:Dogs; D006454:Hemoglobins / Q000378:metabolism*; D006790:Host-Parasite Interactions; D006801:Humans; D008954:Models, Biological; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D016415:Sequence Alignment; D013379:Substrate Specificity
D006454:Hemoglobins; D016282:Aspartic Acid Endopeptidases; D002402:Cathepsin D