TY - JOUR
T1 - An evolutionary analysis of trypanosomatid GP63 proteases
AU - Ma, Lina
AU - Chen, Kaifu
AU - Meng, Qingshu
AU - Liu, Qingyou
AU - Tang, Petrus
AU - Hu, Songnian
AU - Yu, Jun
N1 - Funding Information:
We are very grateful to Drs. Yingfeng Luo and Dan Qi for their useful suggestions and comments during the study and Mr. Joe Yu for editing the manuscript. The work is supported by a grant from National Science and Technology Key Project (2008ZX1004-013), the Ministry of Science and Technology of the People’s Republic of China.
Copyright:
Copyright 2017 Elsevier B.V., All rights reserved.
PY - 2011/10
Y1 - 2011/10
N2 - The trypanosomatid GP63 proteases are known to be involved in parasite-host interaction and exhibit strong sequence and structural similarities to those of their hosts and insect vectors. Based on genome sequences of the three trypanosomatids, Trypanosoma brucei, Trypanosoma cruzi, and Leishmania spp., we annotated all their GP63 proteases and divided highly duplicated T. cruzi GP63 proteases into four novel groups according to sequence features. In Leishmania spp., we studied the evolutionary dynamics of GP63 proteins and identified 57 amino acid sites that are under significant positive selections. These sites may contribute to the functional variations of the GP63 proteases and provide clues for vaccine development.
AB - The trypanosomatid GP63 proteases are known to be involved in parasite-host interaction and exhibit strong sequence and structural similarities to those of their hosts and insect vectors. Based on genome sequences of the three trypanosomatids, Trypanosoma brucei, Trypanosoma cruzi, and Leishmania spp., we annotated all their GP63 proteases and divided highly duplicated T. cruzi GP63 proteases into four novel groups according to sequence features. In Leishmania spp., we studied the evolutionary dynamics of GP63 proteins and identified 57 amino acid sites that are under significant positive selections. These sites may contribute to the functional variations of the GP63 proteases and provide clues for vaccine development.
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U2 - 10.1007/s00436-011-2348-x
DO - 10.1007/s00436-011-2348-x
M3 - Article
AN - SCOPUS:85027926400
VL - 109
SP - 1075
EP - 1084
JO - Parasitology Research
JF - Parasitology Research
SN - 0932-0113
IS - 4
ER -