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An embryo-associated fatty acid-binding protein in the filarial nematode Brugia malayi.
Mol Biochem Parasitol. 2002 Sep-Oct; 124(1-2):1-10.MB

Abstract

Brugia malayi is a filarial nematode parasite that causes lymphatic filariasis, a disease that affects millions of people in the tropics. Sexual reproduction of filarial worms occurs within the lymphatic vessels of the human host and is crucial for transmission of the parasite to the mosquito vector. We have previously identified several B. malayi genes that exhibit apparent gender-specific expression. One of these had significant sequence similarity to the Ascaris suum embryo-associated fatty acid binding protein, As-p18. The full length cDNA for the B. malayi female-associated fatty acid binding protein (Bm-FAB-1) encodes a 17.8 kDa protein (excluding a signal peptide) with 70% sequence identity with mature As-p18 and significant similarity to Caenorhabditis elegans and mammalian fatty acid-binding proteins (FABPs). Antibodies raised to Bm-FAB-1 bound to developing embryos within female worms, especially around early embryo cells and the surfaces of immature worms within eggs. Functional studies showed that recombinant Bm-FAB-1 binds to several long chain fatty acids including oleate, but not retinol. Taken together, these results demonstrate that Bm-FAB-1 is a member of an unusual nematode-specific, secreted lipid binding protein family. The existence of a novel class of lipid binding proteins in nematode embryos raises the possibility that drugs targeting these proteins could be developed with broad activity against nematode parasites of medical and veterinary importance.

Authors+Show Affiliations

Infectious Diseases Division, Department of Internal Medicine, Washington University School of Medicine, St Louis, MO, USA. michalsk@uwash.eduNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article

Language

eng

PubMed ID

12387845

Citation

Michalski, Michelle L., et al. "An Embryo-associated Fatty Acid-binding Protein in the Filarial Nematode Brugia Malayi." Molecular and Biochemical Parasitology, vol. 124, no. 1-2, 2002, pp. 1-10.
Michalski ML, Monsey JD, Cistola DP, et al. An embryo-associated fatty acid-binding protein in the filarial nematode Brugia malayi. Mol Biochem Parasitol. 2002;124(1-2):1-10.
Michalski, M. L., Monsey, J. D., Cistola, D. P., & Weil, G. J. (2002). An embryo-associated fatty acid-binding protein in the filarial nematode Brugia malayi. Molecular and Biochemical Parasitology, 124(1-2), 1-10.
Michalski ML, et al. An Embryo-associated Fatty Acid-binding Protein in the Filarial Nematode Brugia Malayi. Mol Biochem Parasitol. 2002 Sep-Oct;124(1-2):1-10. PubMed PMID: 12387845.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - An embryo-associated fatty acid-binding protein in the filarial nematode Brugia malayi. AU - Michalski,Michelle L, AU - Monsey,John D, AU - Cistola,David P, AU - Weil,Gary J, PY - 2002/10/22/pubmed PY - 2003/2/1/medline PY - 2002/10/22/entrez SP - 1 EP - 10 JF - Molecular and biochemical parasitology JO - Mol Biochem Parasitol VL - 124 IS - 1-2 N2 - Brugia malayi is a filarial nematode parasite that causes lymphatic filariasis, a disease that affects millions of people in the tropics. Sexual reproduction of filarial worms occurs within the lymphatic vessels of the human host and is crucial for transmission of the parasite to the mosquito vector. We have previously identified several B. malayi genes that exhibit apparent gender-specific expression. One of these had significant sequence similarity to the Ascaris suum embryo-associated fatty acid binding protein, As-p18. The full length cDNA for the B. malayi female-associated fatty acid binding protein (Bm-FAB-1) encodes a 17.8 kDa protein (excluding a signal peptide) with 70% sequence identity with mature As-p18 and significant similarity to Caenorhabditis elegans and mammalian fatty acid-binding proteins (FABPs). Antibodies raised to Bm-FAB-1 bound to developing embryos within female worms, especially around early embryo cells and the surfaces of immature worms within eggs. Functional studies showed that recombinant Bm-FAB-1 binds to several long chain fatty acids including oleate, but not retinol. Taken together, these results demonstrate that Bm-FAB-1 is a member of an unusual nematode-specific, secreted lipid binding protein family. The existence of a novel class of lipid binding proteins in nematode embryos raises the possibility that drugs targeting these proteins could be developed with broad activity against nematode parasites of medical and veterinary importance. SN - 0166-6851 UR - https://www.unboundmedicine.com/medline/citation/12387845/An_embryo_associated_fatty_acid_binding_protein_in_the_filarial_nematode_Brugia_malayi_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0166685102000816 DB - PRIME DP - Unbound Medicine ER -