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Infection and Immunity, October 1998, p. 4924-4931, Vol. 66, No. 10
Division of Experimental and Clinical
Microbiology, Department of Biomedical Sciences, University of
Sassari, Sassari, Italy
Received 27 May 1998/Returned for modification 30 June
1998/Accepted 20 July 1998
We have identified and sequenced a cDNA clone coding for
Trichomonas vaginalis alpha-actinin. Analysis of the
obtained sequence revealed that the 2,857-nucleotide-long cDNA
contained an open reading frame encoding 849 amino acids which showed
consistent homology with alpha-actinins of different species. Such
homology was particularly significant in regions which have been
reported to represent the actin-binding and Ca2+-binding
domains in other alpha-actinins. The deduced protein was also
characterized by the presence of a divergent central region thought to
play a role in its high immunogenicity. A study of protein localization
performed by immunofluorescence revealed that the protein is diffusely
distributed throughout the T. vaginalis cytoplasm when the
cell is pear shaped. When parasites adhere and transform into the
amoeboid morphology, the protein is located only in areas close to the
cytoplasmic membrane and colocalizes with actin. Concomitantly with
transformation into the amoeboid morphology, alpha-actinin mRNA
expression is upregulated.
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
Cloning and Molecular Characterization of a cDNA
Clone Coding for Trichomonas vaginalis Alpha-Actinin and
Intracellular Localization of the Protein
*
Corresponding author. Mailing address: Department of
Biomedical Sciences, Division of Experimental and Clinical
Microbiology, University of Sassari, Viale S. Pietro 43/B, 07100 Sassari, Italy. Phone: 39 79 228301. Fax: 39 79 212345. E-mail:
micropat{at}ssmain.uniss.it.
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