Conservation of primary sequence of gp29, the major soluble cuticular glycoprotein, in three species of lymphatic filariae

Cookson, Edith; Tang, Liang; Selkirk, Murray E.

doi:10.1016/0166-6851(93)90099-j

Cited by 26 publications

(8 citation statements)

References 12 publications

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“…Bp‐ GPX‐1 from Brugia pahangi shows an identical amino acid sequence (25) while that from Wuchereria bancrofti diverges by only 3% (20)(Table 3). However, there are a number of synonomous nucleotide substitutions, with introns diverging by 10% ( B. malayi/B.…”

Section: Adult Surface‐associated Proteinsmentioning

confidence: 99%

Immunological genomics of Brugia malayi: filarial genes implicated in immune evasion and protective immunity

Maizels

Blaxter

Scott

2001

Parasite Immunology

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Filarial nematodes are metazoan parasites with genome sizes of> 100 million base pairs, probably encoding 15 000-20 000 genes. Within this considerable gene complement, it seems likely that filariae have evolved a spectrum of immune evasion products which underpin their ability to live for many years within the human host. Moreover, no suitable vaccine currently exists for human filarial diseases, and few markers have yet been established for diagnostic use. In this review, we bring together biochemical and immunological data on prominent filarial proteins with the exciting new information provided by the Filarial Genome Project's expressed sequence tag (EST) database. In this discussion, we focus on those genes with the highest immunological profile, such as inhibitors of host enzymes, cytokine homologues and stage-specific surface proteins, as well as products associated with the mosquito-borne infective larva which offer the best opportunity for an anti-filarial vaccine. These gene products provide a fascinating glimpse of the molecular repertoire which helminth parasites have evolved to manipulate and evade the mammalian immune response.

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Section: Adult Surface‐associated Proteinsmentioning

confidence: 99%

Immunological genomics of Brugia malayi: filarial genes implicated in immune evasion and protective immunity

Maizels

Blaxter

Scott

2001

Parasite Immunology

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“…Cookson et al, 1992Cookson et al, , 1993reviewed in Henkle-Duhrsen and Kampkotter, 2001). Although GpXs usually play a role in removal of hydrogen peroxide and thus in protection of living tissues against oxidative stress, the role of the secreted GpX in nematodes is uncertain.…”

Section: Introductionmentioning

confidence: 99%

Glutathione peroxidases of the potato cyst nematode Globodera Rostochiensis

Jones¹,

Reavy²,

Smant

et al. 2004

Gene

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“…The cysteine residues were found to be highly conserved in the GPXs of Brugia pahangi , Brugia malayi , Wuchereria bancrofti , and Dirofilaria immitis [8,34]. Therefore, these findings suggest that the GPXs of nematode are selenium-independent.…”

Section: Discussionmentioning

confidence: 99%

Cloning and characterization of a selenium-independent glutathione peroxidase (HC29) from adultHaemonchus contortus

et al. 2012

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The complete coding sequence of Haemonchus (H.) contortus HC29 cDNA was generated by rapid amplification of cDNA ends in combination with PCR using primers targeting the 5'- and 3'-ends of the partial mRNA sequence. The cloned HC29 cDNA was shown to be 1,113 bp in size with an open reading frame of 507 bp, encoding a protein of 168 amino acid with a calculated molecular mass of 18.9 kDa. Amino acid sequence analysis revealed that the cloned HC29 cDNA contained the conserved catalytic triad and dimer interface of selenium-independent glutathione peroxidase (GPX). Alignment of the predicted amino acid sequences demonstrated that the protein shared 44.7~80.4% similarity with GPX homologues in the thioredoxin-like family. Phylogenetic analysis revealed close evolutionary proximity of the GPX sequence to the counterpart sequences. These results suggest that HC29 cDNA is a GPX, a member of the thioredoxin-like family. Alignment of the nucleic acid and amino acid sequences of HC29 with those of the reported selenium-independent GPX of H. contortus showed that HC29 contained different types of spliced leader sequences as well as dimer interface sites, although the active sites of both were identical. Enzymatic analysis of recombinant prokaryotic HC29 protein showed activity for the hydrolysis of H2O2. These findings indicate that HC29 is a selenium-independent GPX of H. contortus.

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Conservation of primary sequence of gp29, the major soluble cuticular glycoprotein, in three species of lymphatic filariae

Cited by 26 publications

References 12 publications

Immunological genomics of Brugia malayi: filarial genes implicated in immune evasion and protective immunity

Immunological genomics of Brugia malayi: filarial genes implicated in immune evasion and protective immunity

Glutathione peroxidases of the potato cyst nematode Globodera Rostochiensis

Cloning and characterization of a selenium-independent glutathione peroxidase (HC29) from adultHaemonchus contortus

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