Journal
EXPERIMENTAL PARASITOLOGY
Volume 118, Issue 1, Pages 129-133Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.exppara.2007.06.012
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Funding
- NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [R01AI059451, R01AI032135, R01AI045540, R01AI067874, R01AI048822] Funding Source: NIH RePORTER
- Veterans Affairs [I01BX000536] Funding Source: NIH RePORTER
- NIAID NIH HHS [R01 AI045540-01A2, R01 AI059451, R01 AI045540, R01 AI067874, R01 AI32135, R01 AI45540, R01 AI059451-01A2, R01 AI032135-08, R01 AI048822, R01 AI032135, R01 AI48822, R01 AI048822-01A1] Funding Source: Medline
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Homogenous metacyclic promastigotes of Leishmania chagasi were isolated by buoyant density from in vitro heterogeneous cultures and used for biochemical characterization of isoforms of the major surface protease (MSP). Compared to stationary phase promastigotes, metacyclic cells had three times more MSP, produced 3-fold higher parasite loads in a mouse model in vivo, and were more resistant to complement-mediated lysis in vitro. These metacyclic L. chagasi expressed both the virulence-associated 59-kDa, and the constitutively expressed 63-kDa, isoforms of MSP. (c) 2007 Elsevier Inc. All rights reserved.
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