
doi: 10.1292/jvms.65.519
pmid: 12736436
For studying protein trafficking in Babesia-infected erythrocyte, we describe the cloning of a Rab5, one of molecular marker for vesicle trafficking in eukaryotic cells, gene homologue in Babesia gibsoni (BgRab5). The full-length cDNA of BgRab5 is 1,020 bp long with an open reading frame encoding a protein of 220 amino acids. The deduced amino acid sequence of BgRab5 contained the highly conserved GTP-binding consensus sequence and shares about 40% homology with that of Rab5 from Plasmodium falciparum, Toxoplasma gondii, Dog, Lotus japonicusor, Oryza sativa. Northern blot analysis showed that the BgRab5 probe hybridized with a 1kb band in total RNA from parasitized erythrocytes, that was consistent with the size of the BgRab5 full-length cDNA.
DNA, Complementary, Base Sequence, Sequence Homology, Amino Acid, Molecular Sequence Data, Babesia, <i>Babesia gibsoni</i>, Dogs, Rab5, Consensus Sequence, cDNA cloning, Animals, Amino Acid Sequence, Cloning, Molecular, Sequence Alignment, Conserved Sequence, rab5 GTP-Binding Proteins
DNA, Complementary, Base Sequence, Sequence Homology, Amino Acid, Molecular Sequence Data, Babesia, <i>Babesia gibsoni</i>, Dogs, Rab5, Consensus Sequence, cDNA cloning, Animals, Amino Acid Sequence, Cloning, Molecular, Sequence Alignment, Conserved Sequence, rab5 GTP-Binding Proteins
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