Myosins of Babesia bovis: Molecular characterisation, erythrocyte invasion, and phylogeny

Lew, A. E., Dluzewski, A. R., Johnson, A. M. and Pinder, J. C. (2002) Myosins of Babesia bovis: Molecular characterisation, erythrocyte invasion, and phylogeny. Cell Motility and the Cytoskeleton, 52 4: 202-220. doi:10.1002/cm.10046

Author Lew, A. E.
Dluzewski, A. R.
Johnson, A. M.
Pinder, J. C.
Title Myosins of Babesia bovis: Molecular characterisation, erythrocyte invasion, and phylogeny
Journal name Cell Motility and the Cytoskeleton   Check publisher's open access policy
ISSN 0886-1544
Publication date 2002-08
Sub-type Article (original research)
DOI 10.1002/cm.10046
Volume 52
Issue 4
Start page 202
End page 220
Total pages 19
Place of publication Hoboken, NJ, United States
Publisher John Wiley & Sons
Language eng
Formatted abstract
Using degenerate primers, three putative myosin sequences were amplified from Australian isolates of Babesa bovis and confirmed as myosins (termed Bbmyo-A, Bbmyo-B, and Bbmyo-C) from in vitro cultures of the W strain of B. bovis. Comprehensive analysis of 15 apicomplexan myosins suggests that members of Class XIV be defined as those with greater than 35% myosin head sequence identity and that these be further subclassed into groups bearing above 50-60% identity. Bbmyo-A protein bears a strong similarity with other apicomplexan myosin-A type proteins (subclass XIVa), the Bbmyo-B myosin head protein sequence exhibits low identity (35-39%) with all members of Class XIV, and 5′-sequence of Bbmyo-C shows strong identity (60%) with P. falciparum myosin-C protein. Domain analysis revealed five divergent IQ domains within the neck of Pfmyo-C, and a myosin-N terminal domain as well as a classical IQ sequence unusually located within the head converter domain of Bbmyo-B. A cross-reacting antibody directed against P. falciparum myosin-A (Pfmyo-A) revealed a zone of approximately 85 kDa in immunoblots prepared with B. bovis total protein, and immunofluorescence inferred stage-specific myosin-A expression since only 25% of infected erythrocytes with mostly paired B. bovis were immuno-positive. Multiplication of B. bovis in in vitro culture was inhibited by myosin- and actin-binding drugs at concentrations lower than those that inhibit P. falciparum. This study identifies and classifies three myosin genes and an actin gene in B. bovis, and provides the first evidence for the participation of an actomyosin-based motor in erythrocyte invasion in this species of apicomplexan parasite.
Keyword Myosin
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collection: Queensland Alliance for Agriculture and Food Innovation
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Citation counts: TR Web of Science Citation Count  Cited 20 times in Thomson Reuters Web of Science Article | Citations
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Created: Mon, 07 Mar 2011, 15:14:10 EST