Comparison of cysteine peptidase activities in Trichobilharzia regenti and Schistosoma mansoni cercariae.

Abstract:

:Cercariae of the bird schistosome Trichobilharzia regenti and of the human schistosome Schistosoma mansoni employ proteases to invade the skin of their definitive hosts. To investigate whether a similar proteolytic mechanism is used by both species, cercarial extracts of T. regenti and S. mansoni were biochemically characterized, with the primary focus on cysteine peptidases. A similar pattern of cysteine peptidase activities was detected by zymography of cercarial extracts and their chromatographic fractions from T. regenti and S. mansoni. The greatest peptidase activity was recorded in both species against the fluorogenic peptide substrate Z-Phe-Arg-AMC, commonly used to detect cathepsins B and L, and was markedly inhibited (> 96%) by Z-Phe-Ala-CHN2 at pH 4.5. Cysteine peptidases of 33 kDa and 33-34 kDa were identified in extracts of T. regenti and S. mansoni cercariae employing a biotinylated Clan CA cysteine peptidase-specific inhibitor (DCG-04). Finally, cercarial extracts from both T. regenti and S. mansoni were able to degrade native substrates present in skin (collagen II and IV, keratin) at physiological pH suggesting that cysteine peptidases are important in the pentration of host skin.

journal_name

Parasitology

journal_title

Parasitology

authors

Kasný M,Mikes L,Dalton JP,Mountford AP,Horák P

doi

10.1017/S0031182007002910

subject

Has Abstract

pub_date

2007-10-01 00:00:00

pages

1599-609

issue

Pt 11

eissn

0031-1820

issn

1469-8161

pii

S0031182007002910

journal_volume

134

pub_type

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