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Table 1 Summary of phenotypes for mutations in the Nef polyproline region

From: Overlapping effector interfaces define the multiple functions of the HIV-1 Nef polyproline helix

Residue Hck SH3 PAK2 MHCI EVI CD4
EEEE/AAAA # +1 1 +1 ++1
V66A # + ++ + ++
G67A # ++
F68A # +
P69A ++3 3,5 ++6 5 ++6
P72G + ++
Q73R ++ ++ + ++
V74I ++ ++ ++ ++
P75G + + ++
L76V ++ + + + ++
R77K ++ ++
P78G ++ + ++ ++
F90A ++ + + ++
D123E # ++2,4 2,4 4 2,4
  1. Results are presented from this report unless otherwise indicated. 1Baugh et al. [29]; 2Kwak et al. [31]; 3Manninen et al. [20]; 4O’Neil et al. [32]; 5Wiskerchen et al. [41]; 6Yamada et al. [33]. Hck SH3, in vitro binding of Nef to Hck SH3 domain; PAK2, Nef/activated PAK2 complex formation; MHCI, MHCI downregulation; EVI, enhancement of virion infectivity; CD4, CD4 downregulation. #, indicates that the residue is outside of the known Nef-Hck SH3 interface [23, 24]; “++” activity of mutated protein is >75% of wild type protein; “+” activity is between 25% and 75% of wild type; “-“ activity is less that 25% of wild type. EEEE/AAAA is the quadruple mutation of the tetra-glutamate segment (amino acids 62–65) of Nef mutated to four alanines.