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PHD : Parasites, Hosts and Diseases

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Serine Proteases of Parasitic Helminths

The Korean Journal of Parasitology 2015;53(1):1-11.
Published online: February 27, 2015

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• Received: March 27, 2014   • Revised: September 15, 2014   • Accepted: October 23, 2014

© 2015, Korean Society for Parasitology and Tropical Medicine

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Serine Proteases of Parasitic Helminths
Korean J Parasitol. 2015;53(1):1-11.   Published online February 27, 2015
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Serine Proteases of Parasitic Helminths
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Fig. 1. The pattern and characterization of the binding pocket responsible for specificity of serine proteases. (A) Trypsin specificity is due to a negatively charged aspartic acid (Asp) located in the base of the binding pocket. Thus, it specifically cleaves peptide bonds of positively charged residues, i.e., lysine (Lys) and arginine (Arg). (B) Chymotrypsin specificity is due to a deep hydrophobic pocket containing serine (Ser) and glycine (Gly). This contributes to specifically cleave peptide bonds of large hydrophobic residues, i.e., phenylalanine (Phe), tryptophan (Trp), and tyrosine (Tyr). (C) Elastase has a much smaller binding pocket containing Arg and Lys than Trypsin or Chymotrypsin and prefers to cleave peptides of small, neutral residues, such as alanine (Ala), glycine (Gly), and valine (Val).
Fig. 2. A schematic illustration of general catalytic mechanism for serine proteases (modified from Mark Brandt, 2001). (A) Substrate binding: substrate binds to the recognition site of the serine protease and exposes the carbonyl of the scissile amide bond. (B) Nucleophilic attack: His 57 attracts the proton from the hydroxyl group of Ser 195 and the Sser 195 attacks the carbonyl of the peptide substrate. (C) Protonation: The amide of peptide subtract accepts a proton from His 57 and dissociates. (D) Deacylation: water molecule attacks the acyl-enzyme complex and catalytic triad is restored.
Serine Proteases of Parasitic Helminths
Species Serine protease Molecular size (kDa) Stage and/or localization Role
T. spiralis TspSP-1/Ts32-2 44.9 Muscle stage Invasion and nurse cell formation
Stichosome of muscle larvae
T. spiralis TsSerP 71.6 All life cycle. Moult and nutrition
Peripheral regions and the oesophagus of T. spiralis muscle larvae and adult worms.
T. spiralis TspSP-1.2 35.5 All life cycle cuticle and internal organs of the muscle larvae. Invasion in intestinal stage
T. spiralis NBL1 Newborn Larvae Cuticles of new born larvae Invasion
T. pudospiralis TppSP-1 50.8 Muscle larvae Unknow
T. muris 85 and 105 Adult worms Nutrition, invasion, and immune evasion
A. simplex 25, 26, and 30 Infective larvae Unknow
A. summ As-TRY-5 46 Adult worm Sperm activation
O. volvulus 40 Microfilariae and adult males Migration
O. lienalis 43 Infective larvae Migration
O. volvulus L3 larvae Unkown
B. malayi Microfilariae Immune evasion
A. caninum 36 Filariform larvae Anticlotting
S. carpocapsae sc-sp-1 27.3 Parasitic stage Invasion
S. carpocapsae sc-sp-3 28.9 Parasitic stage apoptosis
S. carpocapsae Sc-ELA 28.9 Parasitic stage Migration
S. carpocapsae Sc-Trypsin 29 Parasitic stage Immune depression
S. carpocapsae Sc-chymotrypsin 30 Parasitic stage Immune depression
Taxon Species Serine protease Molecular size (kDa) Stage and/or localization Role
Cestode S. mansoni 198 and 104 Plerocercoid Invasion and migration
S. mansoni 36 Plerocercoid Immune evasion
E. granulosus Ag5 60 All stages Unknown
T. solium TsAg5 62.8 Cysticerci Unknown
S. solidus 23.5 Procercoids Invasion
Trematode F. hepatica DPP 200 All stages Nutrition
F. gigantica serine PIc 60 All stages Unknown
S. mansoni SmCE 30 Cercariae and daughter sporocysts Invasion and
Immune evasion
Table 1. Characteristics of serine proteases from parasitic nematodes
Table 2. Characteristics of serine proteases from cestodes and trematodes