Document Detail


Characterisation of a fatty acid and retinol binding protein orthologue from the hookworm Ancylostoma ceylanicum.
MedLine Citation:
PMID:  19591834     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Hookworms, bloodfeeding intestinal nematodes, infect nearly one billion people in resource limited countries and are a leading cause of anaemia and malnutrition. Like other nematodes, hookworms lack the capacity to synthesise essential fatty acids de novo and therefore must acquire those from exogenous sources. The cDNA corresponding to a putative Ancylostoma ceylanicum fatty acid and retinol binding protein-1 (AceFAR-1) was amplified from adult hookworm mRNA. Studies using quantitative reverse transcriptase real-time PCR demonstrate that AceFAR-1 transcripts are most abundant in the earliest developmental stages of the parasite, and greater in females than males. Using in vitro assays, the recombinant AceFAR-1 (rAceFAR-1) was shown to bind individual fatty acids with equilibrium dissociation constants in the low micromolar range. The pattern of fatty acid uptake by live adult worms cultured ex vivo was similar to the in vitro binding profile of rAceFAR-1, raising the possibility that the native protein may be involved in acquisition of fatty acids by A. ceylanicum. Animals vaccinated orally with rAceFAR-1 and the mucosal adjuvant cholera toxin exhibited a statistically significant (40-47%) reduction in intestinal worm burden compared with controls immunized with antigen or adjuvant alone. Together, these data suggest a potential role for AceFAR-1 in hookworm biology, making it a potentially valuable target for drug and vaccine development.
Authors:
Keke C Fairfax; Jon J Vermeire; Lisa M Harrison; Richard D Bungiro; Wayne Grant; Sohail Z Husain; Michael Cappello
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2009-07-08
Journal Detail:
Title:  International journal for parasitology     Volume:  39     ISSN:  1879-0135     ISO Abbreviation:  Int. J. Parasitol.     Publication Date:  2009 Dec 
Date Detail:
Created Date:  2009-10-12     Completed Date:  2011-01-13     Revised Date:  2013-04-16    
Medline Journal Info:
Nlm Unique ID:  0314024     Medline TA:  Int J Parasitol     Country:  England    
Other Details:
Languages:  eng     Pagination:  1561-71     Citation Subset:  IM    
Affiliation:
Infectious Diseases Section and Program in International Child Health, Department of Pediatrics, Yale School of Medicine, New Haven, CT 06520, USA.
Data Bank Information
Bank Name/Acc. No.:
GENBANK/EU449764
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MeSH Terms
Descriptor/Qualifier:
Analysis of Variance
Ancylostoma / growth & development,  metabolism*
Ancylostomatoidea
Animals
Cricetinae
DNA, Complementary / metabolism
Fatty Acids / metabolism*
Female
Life Cycle Stages
Male
Molecular Sequence Data
Retinol-Binding Proteins / metabolism*
Grant Support
ID/Acronym/Agency:
AI007640/AI/NIAID NIH HHS; AI058980/AI/NIAID NIH HHS; AI058980-03S1/AI/NIAID NIH HHS; DK68116/DK/NIDDK NIH HHS; K08 DK068116/DK/NIDDK NIH HHS; R01 AI058980-03/AI/NIAID NIH HHS; R01 AI058980-03S1/AI/NIAID NIH HHS; T32 AI007640-08/AI/NIAID NIH HHS
Chemical
Reg. No./Substance:
0/DNA, Complementary; 0/Fatty Acids; 0/Retinol-Binding Proteins

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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