Open AccessA naturally occurring feline APOBEC3 variant that loses anti-lentiviral activity by lacking two amino acid residues
Author(s) -
Yoriyuki Konno,
Shigetaka Nagaoka,
Izumi Kimura,
Mahoko Takahashi Ueda,
Ryuichi Kumata,
Jumpei Ito,
So Nakagawa,
Tomoko Kobayashi,
Yoshio Koyanagi,
Kei Sato
Publication year - 2018
Publication title -
journal of general virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.55
H-Index - 167
eISSN - 1465-2099
pISSN - 0022-1317
DOI - 10.1099/jgv.0.001046
Subject(s) - biology , haplotype , nonsynonymous substitution , feline immunodeficiency virus , gene , mutagenesis , genetics , amino acid , virology , peptide sequence , microbiology and biotechnology , mutation , virus , lentivirus , allele , genome , viral disease
Apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 3 (APOBEC3) is a mammalian protein that restricts lentiviral replication. Various polymorphisms of mammalian APOBEC3 genes have been observed in humans, Old World monkeys and domestic cats; however, the genetic diversity of APOBEC3 genes in other mammals remains unaddressed. Here we identify a novel haplotype of the feline APOBEC3Z3 gene, an APOBEC3 gene that restricts feline immunodeficiency virus (FIV) replication, in a Eurasian lynx ( Lynx lynx ). Compared to the previously identified lynx APOBEC3Z3 (haplotype I), the new sequence (haplotype II) harbours two amino acid deletions (Q16 and H17) and a nonsynonymous substitution (R68Q). Interestingly, lynx APOBEC3Z3 haplotype II does not suppress FIV infectivity, whereas haplotype I does. Mutagenesis experiments further revealed that deleting two amino acids (Q16 and H17) causes anti-FIV activity loss. This report demonstrates that a naturally occurring APOBEC3 variant loses anti-lentiviral activity through the deletion of two amino acid residues.