D. Bernasconi et al., THE INTERFERON-INDUCED MX-PROTEIN OF CHICKENS LACKS ANTIVIRAL ACTIVITY, Journal of interferon & cytokine research, 15(1), 1995, pp. 47-53
cDNA sequencing revealed that chick Mr protein consists of 705 amino a
cids, Its 84 N-terminal amino acids show no significant sequence homol
ogy to other Mr proteins, They are followed by 514 residues that inclu
de a tripartite GTP binding consensus moth, This region shows 50-70% s
equence identity to mammalian and duck Mr proteins, Sequences near the
C terminus, including a leucine zipper motif, are also conserved, whe
reas the intervening 19 amino acids lack sequence similarity, This uni
que sequence corresponds to a highly variable region in mammalian Mr p
roteins, suggesting that it serves as a spacer between functional doma
ins, Chick and mouse cells transiently transfected with cDNA expressio
n constructs synthesized chick Mr protein at a level that could easily
be detected with specific antibodies, Chick Mr protein in such cells
was mainly cytoplasmic and had a granular appearance, Permanently tran
sfected cell lines expressing high levels of chick Mr protein could no
t be established, suggesting low metabolic stability of chick Mr prote
in or incompatibility with cell proliferation, The antiviral activity
of chick Mr protein was tested at the single-cell level using immunofl
uorescence techniques, Transfected cells expressing chick Mr protein s
howed no enhanced resistance to influenza A virus, vesicular stomatiti
s virus, Thogoto virus, or Sendai virus, Thus, chick Mr joins the list
of Mr proteins without recognized antiviral activity, supporting the
concept that Mr proteins serve unrelated functions.