PMID- 19622410
OWN - NLM
STAT- MEDLINE
DCOM- 20090914
LR  - 20160428
IS  - 2163-6079 (Electronic)
IS  - 0065-308X (Linking)
VI  - 69
DP  - 2009
TI  - Chapter 4. Peptidases of trematodes.
PG  - 205-97
LID - 10.1016/S0065-308X(09)69004-7 [doi]
AB  - Among human and veterinary parasitic diseases the trematodiases (e.g. 
      schistosomiasis, fascioliasis) represent a problem of global importance with vast 
      social, economic and public health impacts, especially in developing countries. 
      Therefore, host-parasite (host-trematode) interactions represent a key topic in 
      many research laboratories, and modern approaches and technologies allow us to 
      study the molecular basis of these interactions. As a consequence, key molecules 
      produced by trematodes in order to ensure parasite invasion and survival within a 
      hosts can be characterized. Trematode peptidases certainly belong to such 
      molecules; as they are indispensable biocatalysts in a number of basal biological 
      processes in trematodes (e.g. tissue invasion/migration, nutrition, immune 
      evasion or other host-parasite interactions). Schistosoma mansoni cercarial 
      elastase (CE) (penetration enzyme), cathepsin B (CB) (mainly nutrition enzyme) 
      and Fasciola hepatica cathepsin L (CL) (nutrition, immune evasion enzyme) are 
      probably the most studied trematode peptidases with well-characterized critical 
      functions. Due to the importance of peptidases in host-parasite interactions they 
      are considered to be promising targets for the development of novel 
      chemotherapeutic drugs and vaccines against a number of trematodiases, including 
      schistosomiasis, fascioliasis, paragonimiasis and opisthorchiasis. The present 
      chapter summarizes the data on the biochemical and molecular features of the 
      major trematode peptidases, and describes their role in trematode biology and 
      host-parasite interactions based on proteolysis (peptidolysis).
FAU - Kasny, Martin
AU  - Kasny M
AD  - Department of Parasitology, Faculty of Science, Charles University in Prague, 
      Prague, Czech Republic.
FAU - Mikes, Libor
AU  - Mikes L
FAU - Hampl, Vladimir
AU  - Hampl V
FAU - Dvorak, Jan
AU  - Dvorak J
FAU - Caffrey, Conor R
AU  - Caffrey CR
FAU - Dalton, John P
AU  - Dalton JP
FAU - Horak, Petr
AU  - Horak P
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Review
PL  - England
TA  - Adv Parasitol
JT  - Advances in parasitology
JID - 0370435
RN  - 0 (Virulence Factors)
RN  - EC 3.4.- (Peptide Hydrolases)
SB  - IM
MH  - Animals
MH  - Host-Parasite Interactions
MH  - Humans
MH  - Peptide Hydrolases/*genetics/*metabolism
MH  - Trematoda/*enzymology
MH  - Trematode Infections/parasitology/veterinary
MH  - Virulence Factors/genetics/metabolism
RF  - 344
EDAT- 2009/07/23 09:00
MHDA- 2009/09/15 06:00
CRDT- 2009/07/23 09:00
PHST- 2009/07/23 09:00 [entrez]
PHST- 2009/07/23 09:00 [pubmed]
PHST- 2009/09/15 06:00 [medline]
AID - S0065-308X(09)69004-7 [pii]
AID - 10.1016/S0065-308X(09)69004-7 [doi]
PST - ppublish
SO  - Adv Parasitol. 2009;69:205-97. doi: 10.1016/S0065-308X(09)69004-7.