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Journal of Virology, March 2002, p. 2543-2547, Vol. 76, No. 5
0022-538X/02/$04.00+0     DOI: 10.1128/jvi.76.5.2543-2547.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Identification of a Type 1 Peroxisomal Targeting Signal in a Viral Protein and Demonstration of Its Targeting to the Organelle

*** K. V. K. Mohan, I. Som, and C. D. Atreya*

Section of Viral Pathogenesis and Vaccine Adverse Reactions, Laboratory of Pediatric and Respiratory Viral Diseases, Division of Viral Products, Center for Biologics Evaluation and Research, Food and Drug Administration, Bethesda, Maryland 20892

Received 20 September 2001/ Accepted 28 November 2001

Peroxisomes are unimembrane, respiratory organelles of the cell. Transport of cellular proteins to the peroxisomal matrix requires a type 1 peroxisomal targeting signal (PTS1) which essentially constitutes a tripeptide from the consensus sequence S/T/A/G/C/N-K/R/H-L/I/V/M/A/F/Y. Although PTS-containing proteins have been identified in eukaryotes, prokaryotes, and parasites, viral proteins with such signals have not been identified so far. We report here the first instance of a virus, the rotavirus, which causes infantile diarrhea worldwide, containing a functional C-terminal PTS1 in one of its proteins (VP4). Analysis of 153 rotavirus VP4-deduced amino acid sequences identified five groups of conserved C-terminal PTS1 tripeptide sequences (SKL, CKL, GKL, CRL, and CRI), of which CRL is represented in approximately 62% of the sequences. Infection of cells by a CRL-containing representative rotavirus (SA11 strain) and confocal immunofluorescence analysis revealed colocalization of VP4 with peroxisomal markers and morphological changes of peroxisomes. Further, transient cellular expression of green fluorescent protein (GFP)-fused VP4CRL resulted in transport of VP4 to peroxisomes, whereas the chimera lacking the PTS1 signal, GFP-VP4{Delta}CRL, resulted in diffuse cytoplasmic staining, suggesting a CRL-dependent targeting of the protein. The present study therefore demonstrates hitherto unreported organelle involvement, specifically of the peroxisomes, in rotaviral infections as demonstrated by using the SA11 strain of rotavirus and opens a new line of investigation toward understanding viral pathogenesis and disease mechanisms.

* Corresponding author. Mailing address: Bldg. 29A, Room 2C-11, HFM-460, CBER/FDA, NIH Campus, 8800 Rockville Pike, Bethesda, MD 20892. Phone: (301) 827-1824. Fax: (301) 827-1825. E-mail: atreya{at}cber.fda.gov.

Journal of Virology, March 2002, p. 2543-2547, Vol. 76, No. 5
0022-538X/02/$04.00+0     DOI: 10.1128/jvi.76.5.2543-2547.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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