Battini J L, Kayman S C, Pinter A, Heard J M, Danos O
Laboratoire Rétrovirus et Transfert Génétique, URA CNRS 1157 Département SIDA et Rétrovirus, Institut Pasteur, Paris, France.
Virology. 1994 Jul;202(1):496-9. doi: 10.1006/viro.1994.1369.
The 243 N-terminal residues of Friend Murine Leukemia Virus envelope glycoprotein (SU) fold into a structurally and functionally autonomous domain which contains the determinants for binding to the ecotropic virus receptor. The two N-linked glycosylation sites present in this N-terminal portion of the viral SU were removed by site-directed mutagenesis without disturbing its biosynthesis and incorporation into infectious virions. A truncated version of the mutant protein which included only the N-terminal domain was poorly transported but still able to interact with the receptor. Interference assays indicated that the interaction between the mutated protein and the virus receptor was weaker. We conclude that the elimination of N-linked oligosaccharide chains in the envelope N-terminal domain do not prevent receptor interaction but results in subtle conformational changes that may alter recognition and binding.
弗瑞德小鼠白血病病毒包膜糖蛋白（SU）的243个N端残基折叠成一个结构和功能自主的结构域，其中包含与亲嗜性病毒受体结合的决定簇。通过定点诱变去除了病毒SU的该N端部分中存在的两个N-连接糖基化位点，而不干扰其生物合成以及其掺入感染性病毒粒子中。仅包含N端结构域的突变蛋白的截短版本转运不佳，但仍能够与受体相互作用。干扰试验表明，突变蛋白与病毒受体之间的相互作用较弱。我们得出结论，包膜N端结构域中N-连接寡糖链的消除并不妨碍受体相互作用，但会导致细微的构象变化，这可能会改变识别和结合。
