Heparin binding proteins from Leishmania ( Viannia) braziliensis promastigotes
We have examined the heparin binding proteins from Leishmania ( Viannia) braziliensis promastigotes (HBP-Lb) by chromatography assays. The proposed strategy to isolate an enriched fraction of the HBP-Lb consisted of an association of the Triton X-114 method with affinity chromatography in heparin-Se...
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Published in: | Veterinary parasitology Vol. 145; no. 3; pp. 234 - 239 |
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Main Authors: | , , , , , , , , |
Format: | Journal Article |
Language: | English |
Published: |
Netherlands
Elsevier B.V
30-04-2007
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Subjects: | |
Online Access: | Get full text |
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Summary: | We have examined the heparin binding proteins from
Leishmania (
Viannia)
braziliensis promastigotes (HBP-Lb) by chromatography assays. The proposed strategy to isolate an enriched fraction of the HBP-Lb consisted of an association of the Triton X-114 method with affinity chromatography in heparin-Sepharose 4B column. SDS-PAGE analysis of the eluted proteins showed two main protein bands (65.0 and 54.5
kDa), while a single protein band was observed in native electrophoresis gel. The hemagglutination property of HBP-Lb over rabbit erythrocytes was confirmed up to 6.3
±
0.5
μg of protein mL
−1. Additionally, we have assayed the potential of HBP-Lb labeled with sulfo-NHS-LC-biotin in binding to nitrocellulose-immobilized gut proteins extracted of
Lutzomyia intermedia and
Lutzomyia whitmani. The results indicated a similar profile of five ligands (67.0, 62.1, 59.5, 56.0 and 47.5
kDa) in both studied
Lutzomyia species. This is the first direct description of this class of protein in
L. (
V.)
braziliensis with a suggestion of its biological activity in the interaction of
Leishmania with
Lutzomyia gut cells, which maybe a crucial step during this parasite's life cycle. |
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Bibliography: | http://dx.doi.org/10.1016/j.vetpar.2006.12.019 ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0304-4017 1873-2550 |
DOI: | 10.1016/j.vetpar.2006.12.019 |