cDNA clones of feline chemokines, MIP-1 alpha, MIP-1 beta and RANTES,
were molecularly isolated with the purpose of using these sequences fo
r future investigation of the inhibitory effects on lentivirus entry a
nd their role in immunological functions. The feline MIP-1 alpha and M
IP-1 beta cDNA clones spanned their entire coding regions encoding 93
and 92 amino acids, respectively. The amino acid sequences of feline M
IP-1 alpha and MIP-1 beta compared to those of their human, mouse and
rat counterparts showed similarities of 75.3-79.6% and 73.9-88.0%, res
pectively. Feline MIP-1 alpha and MIP-1 beta had four conserved cystei
nes with a structure made up of the first two cysteines that are chara
cteristic of the CC-chemokine subfamily. The amino terminal of these M
IP-1 and MIP-1 beta sequences was distinctly hydrophobic, suggesting t
hat they may function as signal peptides. A partial cDNA clone consist
ing of 193 bp was obtained for feline RANTES, and it also showed a hig
h degree of sequence similarity to those of other species and containe
d the characteristic structure made up of adjacent cysteines. These mo
lecular clones of feline chemokines will be useful in the examination
of their inhibitory effect on the cellular entry of feline immunodefic
iency virus. (C) 1998 Elsevier Science B.V. All rights reserved.