Abstract:
:The FAR proteins of nematodes are small ( approximately 20 kDa), helix-rich, fatty acid and retinol-binding (FAR) proteins that appear to be confined to nematodes. We have carried out a comparative sequence and biochemical analysis of selected FAR proteins often species of filarial parasites (from the genera Onchocerca, Brugia, Wuchereria, Loa, Acanthocheilonema and Litomosoides). The sequences fall into two main groups corresponding broadly to the onchocercal and lymphatic filariasis parasites, and only those with unsheathed microfilariae were found to produce glycosylated FAR proteins. The proteins were released into culture medium by all the species and developmental stages investigated. Recombinant forms of two of these proteins (Ov-FAR-1 from O. volvulus and Bm-FAR-1 from B. malayi) were compared for ligand binding in fluorescence-based assays. Both were found to bind all-trans-retinol, (dansylamino) undecanoic acid (DAUDA), and oleic acid by competition. Both produced an identical, and dramatic, blue-shift in the fluorescence emission of DAUDA (from 541 to approximately 483 nm), indicative of similarity in the binding site environments of the two proteins. These findings indicate that there is strong conservation of the biochemical activities of the FAR proteins between the different parasite species, although they appear to have different post-translational modifications which may relate to the biology of the larvae.
journal_name
Mol Biochem Parasitoljournal_title
Molecular and biochemical parasitologyauthors
Garofalo A,Kläger SL,Rowlinson MC,Nirmalan N,Klion A,Allen JE,Kennedy MW,Bradley JEdoi
10.1016/s0166-6851(02)00097-xsubject
Has Abstractpub_date
2002-07-01 00:00:00pages
161-70issue
2eissn
0166-6851issn
1872-9428pii
S016668510200097Xjournal_volume
122pub_type
杂志文章abstract::Evidence is presented that Giardia lamblia and Entamoeba histolytica, phylogenetically unrelated aerotolerant anaerobes, have crucial thiol groups on or easily accessible to their external surface. Both parasites were killed by three structurally unrelated thiol-blocking reagents which penetrate intact cells poorly or...
journal_title:Molecular and biochemical parasitology
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doi:10.1016/0166-6851(84)90096-3
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abstract::Contrary to previous reports in the literature, bloodstream forms of the haemoflagellate protozoan Trypanosoma brucei brucei are not deficient in their ability to metabolize hydrogen peroxide, although they either lack or only possess the normal enzymes for H2O2 detoxification, catalase (EC 1.11.1.6) and glutathione p...
journal_title:Molecular and biochemical parasitology
pub_type: 杂志文章
doi:10.1016/0166-6851(86)90023-x
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doi:10.1016/0166-6851(91)90210-w
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journal_title:Molecular and biochemical parasitology
pub_type: 杂志文章
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journal_title:Molecular and biochemical parasitology
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journal_title:Molecular and biochemical parasitology
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pub_type: 杂志文章
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journal_title:Molecular and biochemical parasitology
pub_type: 杂志文章
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pub_type: 杂志文章
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journal_title:Molecular and biochemical parasitology
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journal_title:Molecular and biochemical parasitology
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journal_title:Molecular and biochemical parasitology
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journal_title:Molecular and biochemical parasitology
pub_type: 杂志文章
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journal_title:Molecular and biochemical parasitology
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journal_title:Molecular and biochemical parasitology
pub_type: 杂志文章
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journal_title:Molecular and biochemical parasitology
pub_type: 杂志文章
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更新日期:1998-05-01 00:00:00
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