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Interactions of HIV-1 Gag with Assembly Cofactors

机译：HIV-1堵嘴与装配辅因子的相互作用

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HIV-1 Gag is the only protein required for retroviral particle assembly.There is evidence suggesting that phosphatidylinositol phosphate and nucleic acid are essential for viruslike particle assembly.To elucidate structural foundations of interactions of HIV-1 Gag with the assembly cofactors PI(4,5)P_2 and RNA,we employed mass spectrometric protein footprinting.In particular,the NHS-biotin modification approach was used to identify the lysine residues that are exposed to the solvent in free Gag and are protected from biotinylation by direct protein-ligand or protein-protein contacts in Gag complexes with PI(4,5)P_2 and/or RNA.Of 21 surface lysines readily modified in free Gag,only K30 and K32,located in the matrix domain,were strongly protected in the Gag-PI(4,5)P_2 complex.Nucleic acid also protected these lysines,but only at significantly higher concentrations.In contrast,nucleic acids and not PI(4,5)P_2 exhibited strong protection of two nucleocapsid domain residues:K391 and K424.In addition,K314,located in the capsid domain,was specifically protected only in the presence of both PI(4,5)P2 and nucleic acid.We suggest that concerted binding of PI(4,5)P_2 and nucleic acid to the matrix and nucleocapsid domains,respectively,promotes protein-protein interactions involving capsid domains.These protein-protein interactions must be involved in virus particle assembly.
机译：HIV-1 Gag是逆转录病毒颗粒组装所需的唯一蛋白质。有证据表明，磷脂酰肌醇磷酸和核酸对于病毒样颗粒组装至关重要。阐明HIV-1 Gag与组装辅因子PI（4， 5）P_2和RNA，我们采用质谱蛋白质印迹法。特别是，使用NHS-生物素修饰方法来鉴定赖氨酸残基，这些赖氨酸残基暴露于游离Gag的溶剂中，并被直接的蛋白质-配体或蛋白质保护免受生物素化作用-蛋白在Gag与PI（4,5）P_2和/或RNA的复合物中的接触。在自由Gag中容易修饰的21个表面赖氨酸中，只有位于基质域中的K30和K32在Gag-PI中得到了强有力的保护（4 ，5）P_2络合物。核酸也可以保护赖氨酸，但浓度要高得多。相反，核酸而不是PI（4,5）P_2则对两个核衣壳域残基K391和K424具有强保护作用。此外，位于衣壳结构域的K314仅在PI（4,5）P2和核酸同时存在时受到特异性保护。我们建议PI（4,5）P_2和核酸协同结合至基质和核衣壳结构域分别促进涉及衣壳结构域的蛋白质-蛋白质相互作用。这些蛋白质-蛋白质相互作用必须参与病毒颗粒的组装。

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