Back to Search Start Over

Angiogenic activity of an Onchocerca volvulus Ancylostoma secreted protein homologue.

Authors :
Higazi TB
Pearlman E
Whikehart DR
Unnasch TR
Source :
Molecular and biochemical parasitology [Mol Biochem Parasitol] 2003 Jun; Vol. 129 (1), pp. 61-8.
Publication Year :
2003

Abstract

Angiogenesis is an important step in the development of ocular onchocercaisis. In previous studies, it has been demonstrated that Onchocerca volvulus homologues of the Ancylostoma secreted protein family have pronounced angiogenic activity. The overall goal of the current study was to determine if this angiogenic effect is exerted through a direct or indirect mechanism. These studies focused on one member of this family, OvASP-2, as this protein is expressed in microfilaria, the stage of the parasite that causes ocular onchocercaisis. Clones encoding truncated and full length open reading frames were expressed as fusion proteins with Escherichia coli maltose binding protein (MBP), and angiogenic activity was compared in vitro and in vivo with MBP alone. Truncated constructs expressing only the first 105 amino acids of OvASP-2 were as active as the full length protein in inducing new blood vessel formation. The full length fusion protein did not stimulate proliferation or production of vascular endothelial growth factor in vascular endothelial cells in vitro, indicating that OvASP-2 does not directly stimulate angiogenesis. Sequence analysis demonstrated that the gene encoding OvASP-2 contained five introns. Sequence comparisons of the genomic loci from West African blinding and non-blinding strains of O. volvulus revealed that some polymorphism existed among the various isolates tested. However, none of these polymorphisms could be used to differentiate the parasite strains, suggesting that qualitative variation in OvASP-2 could not explain the difference in ocular pathogenic potential of the two parasite strains.

Details

Language :
English
ISSN :
0166-6851
Volume :
129
Issue :
1
Database :
MEDLINE
Journal :
Molecular and biochemical parasitology
Publication Type :
Academic Journal
Accession number :
12798507
Full Text :
https://doi.org/10.1016/s0166-6851(03)00094-x