Gerhard W, Haberman A M, Scherle P A, Taylor A H, Palladino G, Caton A J
Wistar Institute of Anatomy and Biology, Philadelphia, Pennsylvania 19104-4268.
J Virol. 1991 Jan;65(1):364-72. doi: 10.1128/JVI.65.1.364-372.1991.
Eight nonoverlapping regions of the hemagglutinin (HA) molecule of influenza virus A/PR/8/34 (PR8), which serve as recognition sites for class II-restricted T cells (TH) from BALB/c mice, have been identified in the form of 10- to 15-amino-acid-long synthetic peptides. These TH determinants are located between residues 110 to 313 of the HA1 polypeptide. From a total of 36 HA-specific TH clones and limiting-dilution cultures of independent clonal origins, 33 (90%) responded to stimulation with one of these peptides. The residual three TH clones appeared to recognize a single additional determinant on the HA1 polypeptide which could not be isolated, however, in the form of a stimulatory peptide. None of the motifs that have been proposed to typify TH determinants were displayed by more than half of these recognition sites. Most unexpected was the finding that none of the TH determinants was located in the ectodomain of the HA2 polypeptide that makes up roughly one-third of the HA molecule. Possible reasons for the preferential recognition of HA1 as opposed to HA2 by TH are discussed.
甲型流感病毒A/PR/8/34（PR8）血凝素（HA）分子的八个不重叠区域已被鉴定为10至15个氨基酸长的合成肽形式，这些区域是来自BALB/c小鼠的II类限制性T细胞（TH）的识别位点。这些TH决定簇位于HA1多肽的110至313位氨基酸残基之间。在总共36个HA特异性TH克隆以及独立克隆来源的有限稀释培养物中，33个（90%）对这些肽之一的刺激有反应。其余三个TH克隆似乎识别HA1多肽上的一个额外决定簇，然而，该决定簇无法以刺激肽的形式分离出来。超过一半的这些识别位点未显示出已被提议作为TH决定簇典型特征的基序。最出乎意料的是，没有一个TH决定簇位于构成HA分子约三分之一的HA2多肽的胞外结构域中。讨论了TH优先识别HA1而非HA2的可能原因。
