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Serine proteases of parasitic helminths.

Yang Y, Wen Yj, Cai YN, Vallée I, Boireau P, Liu MY, Cheng SP - Korean J. Parasitol. (2015)

Bottom Line: Serine proteases form one of the most important families of enzymes and perform significant functions in a broad range of biological processes, such as intra- and extracellular protein metabolism, digestion, blood coagulation, regulation of development, and fertilization.In this review, we described the serine proteases that have been identified in parasitic helminths, including nematodes (Trichinella spiralis, T. pseudospiralis, Trichuris muris, Anisakis simplex, Ascaris suum, Onchocerca volvulus, O. lienalis, Brugia malayi, Ancylostoma caninum, and Steinernema carpocapsae), cestodes (Spirometra mansoni, Echinococcus granulosus, and Schistocephalus solidus), and trematodes (Fasciola hepatica, F. gigantica, and Schistosoma mansoni).Moreover, the possible biological functions of these serine proteases in the endogenous biological phenomena of these parasites and in the host-parasite interaction were also discussed.

View Article: PubMed Central - PubMed

Affiliation: State Key Laboratory for Molecular Biology of Special Economic Animals, Institute of Special Economic Animal and Plant Sciences, Chinese Academy of Agricultural Sciences, Changchun, China ; ANSES, ENVA, UPVM, PRES Paris Est, JRU BIPAR, Animal Health Laboratory, Maisons-Alfort, France.

ABSTRACT
Serine proteases form one of the most important families of enzymes and perform significant functions in a broad range of biological processes, such as intra- and extracellular protein metabolism, digestion, blood coagulation, regulation of development, and fertilization. A number of serine proteases have been identified in parasitic helminths that have putative roles in parasite development and nutrition, host tissues and cell invasion, anticoagulation, and immune evasion. In this review, we described the serine proteases that have been identified in parasitic helminths, including nematodes (Trichinella spiralis, T. pseudospiralis, Trichuris muris, Anisakis simplex, Ascaris suum, Onchocerca volvulus, O. lienalis, Brugia malayi, Ancylostoma caninum, and Steinernema carpocapsae), cestodes (Spirometra mansoni, Echinococcus granulosus, and Schistocephalus solidus), and trematodes (Fasciola hepatica, F. gigantica, and Schistosoma mansoni). Moreover, the possible biological functions of these serine proteases in the endogenous biological phenomena of these parasites and in the host-parasite interaction were also discussed.

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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).
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f1-kjp-53-1-1: 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).

Mentions: Serine proteases are named because of the presence of a nucleophilic serine residue at the active site. The serine residue plays important roles in mediating protein hydrolysis. Most members of the serine proteases contain 3 essential residues at their active sites: a serine (Ser), a histidine (His), and an aspartate (Asp). Although these 3 residues do not have continual distribution throughout the linear protein sequence, they are close to each other in the active 3-dimensional conformation. Chymotrypsin, which is a major serine protease, is found in helminths. Chymotrypsin can be divided into 3 main subfamilies based on its substrate specificity; trypsin-like, chymotrypsin-like, and elastase-like. The proteases in these 3 subfamilies share a similar tertiary structure, but their substrate cleavage specificities differ; trypsin-like, in which a cleavage of amide substrates follows Arg or Lys at the P1 position (Fig. 1A); chymotrypsin-like, in which a cleavage occurs following 1 of the hydrophobic amino acids at P1 (Fig. 1B); and elastase-like, in which a cleavage follows an Ala at P1 (Fig. 1C).


Serine proteases of parasitic helminths.

Yang Y, Wen Yj, Cai YN, Vallée I, Boireau P, Liu MY, Cheng SP - Korean J. Parasitol. (2015)

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).
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4384789&req=5

f1-kjp-53-1-1: 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).
Mentions: Serine proteases are named because of the presence of a nucleophilic serine residue at the active site. The serine residue plays important roles in mediating protein hydrolysis. Most members of the serine proteases contain 3 essential residues at their active sites: a serine (Ser), a histidine (His), and an aspartate (Asp). Although these 3 residues do not have continual distribution throughout the linear protein sequence, they are close to each other in the active 3-dimensional conformation. Chymotrypsin, which is a major serine protease, is found in helminths. Chymotrypsin can be divided into 3 main subfamilies based on its substrate specificity; trypsin-like, chymotrypsin-like, and elastase-like. The proteases in these 3 subfamilies share a similar tertiary structure, but their substrate cleavage specificities differ; trypsin-like, in which a cleavage of amide substrates follows Arg or Lys at the P1 position (Fig. 1A); chymotrypsin-like, in which a cleavage occurs following 1 of the hydrophobic amino acids at P1 (Fig. 1B); and elastase-like, in which a cleavage follows an Ala at P1 (Fig. 1C).

Bottom Line: Serine proteases form one of the most important families of enzymes and perform significant functions in a broad range of biological processes, such as intra- and extracellular protein metabolism, digestion, blood coagulation, regulation of development, and fertilization.In this review, we described the serine proteases that have been identified in parasitic helminths, including nematodes (Trichinella spiralis, T. pseudospiralis, Trichuris muris, Anisakis simplex, Ascaris suum, Onchocerca volvulus, O. lienalis, Brugia malayi, Ancylostoma caninum, and Steinernema carpocapsae), cestodes (Spirometra mansoni, Echinococcus granulosus, and Schistocephalus solidus), and trematodes (Fasciola hepatica, F. gigantica, and Schistosoma mansoni).Moreover, the possible biological functions of these serine proteases in the endogenous biological phenomena of these parasites and in the host-parasite interaction were also discussed.

View Article: PubMed Central - PubMed

Affiliation: State Key Laboratory for Molecular Biology of Special Economic Animals, Institute of Special Economic Animal and Plant Sciences, Chinese Academy of Agricultural Sciences, Changchun, China ; ANSES, ENVA, UPVM, PRES Paris Est, JRU BIPAR, Animal Health Laboratory, Maisons-Alfort, France.

ABSTRACT
Serine proteases form one of the most important families of enzymes and perform significant functions in a broad range of biological processes, such as intra- and extracellular protein metabolism, digestion, blood coagulation, regulation of development, and fertilization. A number of serine proteases have been identified in parasitic helminths that have putative roles in parasite development and nutrition, host tissues and cell invasion, anticoagulation, and immune evasion. In this review, we described the serine proteases that have been identified in parasitic helminths, including nematodes (Trichinella spiralis, T. pseudospiralis, Trichuris muris, Anisakis simplex, Ascaris suum, Onchocerca volvulus, O. lienalis, Brugia malayi, Ancylostoma caninum, and Steinernema carpocapsae), cestodes (Spirometra mansoni, Echinococcus granulosus, and Schistocephalus solidus), and trematodes (Fasciola hepatica, F. gigantica, and Schistosoma mansoni). Moreover, the possible biological functions of these serine proteases in the endogenous biological phenomena of these parasites and in the host-parasite interaction were also discussed.

Show MeSH
Related in: MedlinePlus