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.
Yatsuda
Ana P
AP
Division of Infection Biology, Department of Infectious Diseases and Immunology, Utrecht University, Yalelaan, 1, 3584CL, Utrecht, The Netherlands.
Bakker
Nicole
N
Krijgsveld
Jeroen
J
Knox
David P
DP
Heck
Albert J R
AJ
de Vries
Erik
E
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