Journal of General Virology, Vol 80, 525-535, Copyright © 1999 by Society for General Microbiology

ARTICLES

Nuclear and nucleolar localization of an African swine fever virus protein, I14L, that is similar to the herpes simplex virus-encoded virulence factor ICP34.5

LC Goatley, MB Marron, SC Jacobs, JM Hammond, JE Miskin, CC Abrams, GL Smith and LK Dixon
Institute for Animal Health, Pirbright Laboratory, Woking, Surrey, UK.

PCR analysis of the genomes of 18 different African swine fever virus (ASFV) isolates showed that the I14L open reading frame (ORF) was present as either a long form or short form in all of the isolates. Sequencing of the ORF from eight isolates confirmed that both forms of the ORF were well conserved. Antisera raised against the I14L protein identified the long form of the protein as a 21 kDa protein expressed late during ASFV infection. Immunofluorescent analysis of transiently expressed haemagglutinin-tagged forms of the I14L protein showed that the long form of the protein localized predominantly to the nucleus and within the nucleoli. In contrast, although the short form of the protein was also present predominantly in the nucleus, it did not localize to the nucleoli. Deletion of the N-terminal 14 amino acids from the long form of the I14L protein, which includes a high proportion of basic Arg/Lys residues, abolished the specific nucleolar localization of the protein, although the protein was still present in the nucleus. Addition of this 14 amino acid sequence to beta- galactosidase or replacement of the N-terminal 14 amino acids of the I14L short form with those from the long form directed both of these modified proteins to the nucleolus. This indicates that this 14 amino acid sequence contains all the signals required for nucleolar localization.

This article has been cited by other articles:

				J. Rivera, C. Abrams, B. Hernaez, A. Alcazar, J. M. Escribano, L. Dixon, and C. Alonso The MyD116 African Swine Fever Virus Homologue Interacts with the Catalytic Subunit of Protein Phosphatase 1 and Activates Its Phosphatase Activity J. Virol., March 15, 2007; 81(6): 2923 - 2929. [Abstract] [Full Text] [PDF]

				A. Eulalio, I. Nunes-Correia, A. L. Carvalho, C. Faro, V. Citovsky, S. Simoes, and M. C. Pedroso de Lima Two African Swine Fever Virus Proteins Derived from a Common Precursor Exhibit Different Nucleocytoplasmic Transport Activities J. Virol., September 15, 2004; 78(18): 9731 - 9739. [Abstract] [Full Text] [PDF]

				X. Jing, M. Cerveny, K. Yang, and B. He Replication of Herpes Simplex Virus 1 Depends on the {gamma}134.5 Functions That Facilitate Virus Response to Interferon and Egress in the Different Stages of Productive Infection J. Virol., July 15, 2004; 78(14): 7653 - 7666. [Abstract] [Full Text] [PDF]

				H. Mao and K. S. Rosenthal An N-terminal Arginine-rich Cluster and a Proline-Alanine-Threonine Repeat Region Determine the Cellular Localization of the Herpes Simplex Virus Type 1 ICP34.5 Protein and Its Ligand, Protein Phosphatase 1 J. Biol. Chem., March 22, 2002; 277(13): 11423 - 11431. [Abstract] [Full Text] [PDF]

				S. Goodbourn, L. Didcock, and R. E. Randall Interferons: cell signalling, immune modulation, antiviral response and virus countermeasures J. Gen. Virol., October 1, 2000; 81(10): 2341 - 2364. [Full Text]