Identification of secreted cysteine proteases from the parasitic nematode Haemonchus contortus detected by biotinylated inhibitors.
Seven cathepsin B-like cysteine proteases (CBLs) were identified from the immunoprotective excretory-secretory products of Haemonchus contortus. Two-dimensional (2-D) zymography and biotinylated inhibitors were employed to localize active CBLs in 2-D protein gels. Mass spectrometry provided the identification of AC-4, HMCP1, HMCP2, and GCP7 as well as three novel CBLs encoded by clustered expressed sequence tags.
Division of Infection Biology, Department of Infectious Diseases and Immunology, Utrecht University, Yalelaan, 1, 3584CL, Utrecht, The Netherlands.
Ana P
AP
Yatsuda
Nicole
N
Bakker
Jeroen
J
Krijgsveld
David P
DP
Knox
Albert J R
AJ
Heck
Erik
E
de Vries
D000595:Amino Acid Sequence; D000818:Animals; D019921:Biotinylation / Q000379:methods*; D003546:Cysteine Endopeptidases / Q000302:isolation & purification* / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D006188:Haemonchiasis; D006189:Haemonchus / Q000201:enzymology*; D015801:Helminth Proteins / Q000302:isolation & purification / Q000378:metabolism*; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D016415:Sequence Alignment
D015801:Helminth Proteins; D003546:Cysteine Endopeptidases