Identification of a coronin-like protein in Babesia species.

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Nelly

http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve & db=pubmed & dopt=Abstract & list_uids=15604480 & query_hl=1

Ann N Y Acad Sci. 2004 Oct;1026:125-38.

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Identification of a coronin-like protein in Babesia species.Figueroa JV, Precigout E, Carcy B, Gorenflot A.CENID-PAVET, INIFAP, Juitepec, Morelos, Mexico. figueroa.julio@...The present study was designed to immunochemically identify a coronin-like protein in Babesia bovis, B. bigemina, B. divergens, and B. canis. A 2-kbp cDNA insert of B. bovis carried by plasmid BvN9 was sequenced by the dideoxichain-termination method on both strands. The cDNA insert contained a 1719-bp long open reading frame coding for a deduced protein sequence of 61.7 kDa. Sequence analysis using the PSI-BLAST program revealed about 30% protein sequence identity with a coronin-like protein of Plasmodium falciparum. The encoding sequence of the cDNA insert lacking 70 amino acids at the N-terminal was subcloned in frame into pGEX 4T-3 to produce a recombinant glutathione S-transferase (GST)-pBv fusion protein. Polyclonal antibodies prepared in rabbits immunized with the purified GST-fusion protein recognized a Babesia-specific component of approximately 60 kDa by immunoprecipitation with [35S]methionine-labeled parasites. However, two molecules with relative sizes of 60 and 70 kDa were recognized in Babesia-infected erythrocyte extracts by immunobloting analysis. The 70-kDa component was apparently of host erythrocyte origin. In an indirect fluorescent antibody test, the rabbit serum strongly reacted with the merozoite stage of the four Babesia species, but also, although weakly, with the host erythrocyte. A cosedimentation assay performed with GST-pBv fusion protein and exogenous actin from rabbit liver showed that the GST-pBv fusion protein, but not the GST protein, was associated to actin. From these results, we conclude that the protein present in the four Babesia species analyzed here may be considered as a novel coronin-like, actin-binding protein.PMID: 15604480 [PubMed - indexed for MEDLINE]

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Nelly:

I haven't seen this paper, and am not familiar with coronin binding

proteins.

It looks like they've (maybe) found another protein that human make

antibodies to ( in all species of Babs )

http://data.cellmigration.org/cmckb/report.cgi?

report=fam_overview & fam_acc=coronin

Barb

> Barb? Others?

>

> Any opinions on this?

>

> Nelly

>

> http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?

cmd=Retrieve & db=pubmed & dopt=Abstract & list_uids=15604480 & query_hl=1

>

> Ann N Y Acad Sci. 2004 Oct;1026:125-38. Related Articles,

Links

>

>

> Identification of a coronin-like protein in Babesia species.

>

> Figueroa JV, Precigout E, Carcy B, Gorenflot A.

>

> CENID-PAVET, INIFAP, Juitepec, Morelos, Mexico. figueroa.julio@i...

>

> The present study was designed to immunochemically identify a

coronin-like protein in Babesia bovis, B. bigemina, B. divergens, and

B. canis. A 2-kbp cDNA insert of B. bovis carried by plasmid BvN9 was

sequenced by the dideoxichain-termination method on both strands. The

cDNA insert contained a 1719-bp long open reading frame coding for a

deduced protein sequence of 61.7 kDa. Sequence analysis using the PSI-

BLAST program revealed about 30% protein sequence identity with a

coronin-like protein of Plasmodium falciparum. The encoding sequence

of the cDNA insert lacking 70 amino acids at the N-terminal was

subcloned in frame into pGEX 4T-3 to produce a recombinant

glutathione S-transferase (GST)-pBv fusion protein. Polyclonal

antibodies prepared in rabbits immunized with the purified GST-fusion

protein recognized a Babesia-specific component of approximately 60

kDa by immunoprecipitation with [35S]methionine-labeled parasites.

However, two molecules with relative sizes of 60 and 70 kDa were

recognized in Babesia-infected erythrocyte extracts by immunobloting

analysis. The 70-kDa component was apparently of host erythrocyte

origin. In an indirect fluorescent antibody test, the rabbit serum

strongly reacted with the merozoite stage of the four Babesia

species, but also, although weakly, with the host erythrocyte. A

cosedimentation assay performed with GST-pBv fusion protein and

exogenous actin from rabbit liver showed that the GST-pBv fusion

protein, but not the GST protein, was associated to actin. From these

results, we conclude that the protein present in the four Babesia

species analyzed here may be considered as a novel coronin-like,

actin-binding protein.

>

> PMID: 15604480 [PubMed - indexed for MEDLINE]