Characterization of novel fucosyl- and tyvelosyl-containing glycoconjugates from Trichinella spiralis muscle stage larvae

Wisnewski, Nancy; McNeil, Michael; Grieve, Robert B.; Wassom, Donald L.

doi:10.1016/0166-6851(93)90155-q

Cited by 91 publications

(44 citation statements)

References 41 publications

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“…The expressed product reacted with five sera from mice infected with different Trichinella strains. result was in accord with earlier studies (Song et al, 1994;Zhu et al, 1998 (Denkers et al, 1990;Wisnewski et al, 1993;Yan et al, 1997). In theory, it is possible that the products expressed by E. coli, as diagnostic antigen for trichinellosis, may not be recognized by Trichinellainfected sera due to the lack of glycosylation.…”

Section: Discussionsupporting

confidence: 83%

Study of the 49 kDa excretory-secretory protein gene of Trichinella nativa and Trichinella spiralis

Zheng¹,

Xiao

Wang

et al. 2007

Helminthologia

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SummaryTo study the function of the 49 kDa excretory-secretory (ES) protein gene (P49) of Trichinella, the genes was amplified by RT-PCR from RNA of Trichinella spiralis and Trichinella nativa and several Chinese Trichinella isolates of domestic animals, and sequenced after being cloned. The amplified products of these parasites produced bands of about 950 bp. The 97.2 % to 100 % nucleotides identity and 94.3 % to 100 % identity of deduced amino acids among P49 gene of these Trichinella strains showed the close relationship of these parasites. The P49 gene of T. nativa was cloned into the BamHI site of the prokaryotic expression vector pET-30a, and the recombinant vector was expressed. The expressed product was 40.8 kDa in size. In Western blot analysis, the expressed product was reactive to sera of mice infected with T. nativa, T. spiralis and their Chinese geographical strains.

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Section: Discussionsupporting

confidence: 83%

Study of the 49 kDa excretory-secretory protein gene of Trichinella nativa and Trichinella spiralis

Zheng¹,

Xiao

Wang

et al. 2007

Helminthologia

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“…High level of Nacetyleglucoseamine (GlcNAc) as a major component of the total glycan pool has been described for other helminthes. However, some common structures reported in several parasitic helminthes, such as the LeX epitope, mannose and multi-fucosylated termini (Wisnewski et al 1993;Haslam et al 1996Haslam et al , 1998Haslam et al , 2003Wuhrer et al 2006b andHokke et al 2007), were not found in the current isolated glycoprotein fraction. The interpretation of this observation confirms that at the level of structural characterization, there is a common compound between some parasites as GlcNAc but not necessarily occurred in all helminths which proved existence of unique structure (van Die and Cummings, 2010) of Fasciola [Ser-(Arg-Ser-ArgSer-GlucNAc) 19 -GlucNAc] not necessarily exist in other helminths.…”

Section: Discussionmentioning

confidence: 86%

The role of Ser-(Arg-Ser-Arg-Ser-GlucNAc)19-GlucNAc Fasciola gigantica glycoprotein in the diagnosis of prepatent fasciolosis in rabbits

Abdel-Rahman¹,

Mohamed

Abdel‐Rahman

et al. 2014

J Parasit Dis

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In the present study, the carbohydrate structures associated with Fasciola gigantica adult worm were identified by indirect hemagglutination inhibition test. Glucose was found to be the main monosaccharide associated with the fluke. According to indirect hemagglutination inhibition results, purification of glycoprotein fractions from worm crude extract was carried out by affinity chromatography immobilized glucose agarose gel and Con-A lectin columns. The isolated glycoprotein fractions, FI and FII, were characterized by SDS-PAGE which revealed one band in FI of 26 kDa and another one band of 19.5 kDa in FII compared with 12 bands associated with whole worm extract. Both fractions were also characterized by isoelectric focusing technique which proved that both bands were acidic in nature with pIs 6.4 and 6.5 respectively. The comparative diagnostic evaluation of the two isolated glycoprotein fractions and crude extract of experimental fasciolosis in rabbits by ELISA revealed that FII was more potent in the diagnosis during prepatent (first week post infection) and patent periods (10 weeks post infection) than FI and crude extract. Moreover, infected rabbit sera at ten weeks post infection identified both bands; 26 and 19.5 kDa in western blot analysis confirming its immunodiagnostic activities which was proved previously by ELISA. FII proved potency in diagnosis of fasciolosis in 200 buffalo serum samples of different ages and sexes using ELISA which recorded 95 % positive and 5 % negative samples. Moreover, the detailed structural analyses of the most potent fraction, F11, using mass spectrum was made and elucidated chemical structure; O-glycan [Ser-(Arg-Ser-Arg-Ser-GlucNAc) 19 -GlucNAc]. The present result introduces GlucNAc rich fraction of F .gigantica that can be used successfully in the diagnosis of acute and chronic fasciolosis.

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“…These antigens are released from the encysted muscle larvae (L1) and they continuously stimulate the host immune response (Bruschi 2002). The 45-kDa, 49-kDa and 53-kDa glycoproteins that form the Trichinella-specific triad are tyvelose-bearing antigens that are important during the intestinal phase of the infection (Wisnewski et al 1993, Arasu et al 1994, Romarís et al 2002. These glycoproteins are also responsible for inducing host immunity, as they induce a powerful antibody response against tyvelose that results in the expulsion of the parasite and the protection of the host from reinfection (Appleton et al 1991).…”

Section: Discussionmentioning

confidence: 99%

Trichinella spiralis shares epitopes with human autoantigens

Radović

Gruden-Movsesijan

Ilić

et al. 2012

Mem. Inst. Oswaldo Cruz

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Characterization of novel fucosyl- and tyvelosyl-containing glycoconjugates from Trichinella spiralis muscle stage larvae

Cited by 91 publications

References 41 publications

Study of the 49 kDa excretory-secretory protein gene of Trichinella nativa and Trichinella spiralis

Study of the 49 kDa excretory-secretory protein gene of Trichinella nativa and Trichinella spiralis

The role of Ser-(Arg-Ser-Arg-Ser-GlucNAc)19-GlucNAc Fasciola gigantica glycoprotein in the diagnosis of prepatent fasciolosis in rabbits

Trichinella spiralis shares epitopes with human autoantigens

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