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Antimicrobial Agents and Chemotherapy, August 2004, p. 2993-2998, Vol. 48, No. 8
0066-4804/04/$08.00+0     DOI: 10.1128/AAC.48.8.2993-2998.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Nucleotide and Amino Acid Polymorphisms at Drug Resistance Sites in Non-B-Subtype Variants of Human Immunodeficiency Virus Type 1

Dan Turner,¹ Bluma Brenner,¹ Daniela Moisi,¹ Mervi Detorio,¹ Raymond Cesaire,² Takashi Kurimura,³ Haruyo Mori,⁴ Max Essex,^5,6 Shlomo Maayan,⁷ and Mark A. Wainberg^1*

McGill University AIDS Centre, Lady Davis Institute, Jewish General Hospital, Montreal, Quebec, Canada,¹ Laboratoire de Virologie-Immunologie, Centre Hospitalier Universitaire de Fort-de-France, Fort-de-France, Martinique,² Laboratory of Pathology, Osaka Prefectural Institute of Public Health,⁴ Osaka University, Osaka, Japan,³ Harvard School of Public Health, Boston, Massachusetts,⁵ Harvard Botswana Laboratory, Gaborone, Botswana,⁶ Department of Infectious Diseases, Hadassah Hospital, Jerusalem, Israel⁷

Received 5 January 2004/ Returned for modification 18 March 2004/ Accepted 19 April 2004

We have compared nucleotide substitutions and polymorphisms at codons known to confer drug resistance in subtype B strains of human immunodeficiency virus type 1 (HIV-1) with similar substitutions in viruses of other subtypes. Genotypic analysis was performed on viruses from untreated individuals. Nucleotide and amino acid diversity at resistance sites was compared with a consensus subtype B reference virus. Among patients with non-subtype B infections, polymorphisms relative to subtype B were observed at codon 10 in protease (PR). These included silent substitutions (CTCCTT, CTA, TTA) and an amino acid mutation, L10I. Subtype A viruses possessed a V179I substitution in reverse transcriptase (RT). Subtype G viruses were identified by silent substitutions at codon 181 in RT (TATTAC). Similarly, subtype A/G viruses were identified by a substitution at position 67 in RT (GACGAT). Subtype C was distinguished by silent substitutions at codons 106 (GTAGTG) and 219 (AAAAAG) in RT and codon 48 (GGGGGA) in PR. Variations relative to subtype B were seen at RT position 215 (ACCACT) for subtypes A and A/E. These substitutions and polymorphisms reflect different patterns of codon usage among viruses of different subtypes. However, the existence of different subtypes may only rarely affect patterns of drug resistance-associated mutations.

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* Corresponding author. Mailing address: 3755, Chemin de la Côte Ste-Catherine, Montréal, Québec H3T 1E2, Canada. Phone: (514) 340-8260. Fax: (514) 340-7537. E-mail: mark.wainberg{at}mcgill.ca.

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Antimicrobial Agents and Chemotherapy, August 2004, p. 2993-2998, Vol. 48, No. 8
0066-4804/04/$08.00+0     DOI: 10.1128/AAC.48.8.2993-2998.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

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