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首页> 外文期刊>Molecular and Cellular Biology >Signal processing, glycosylation, and secretion of mutant hemagglutinins of a human influenza virus by Saccharomyces cerevisiae.
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Signal processing, glycosylation, and secretion of mutant hemagglutinins of a human influenza virus by Saccharomyces cerevisiae.

机译：酿酒酵母对人流感病毒的信号处理，糖基化和突变血凝素的分泌。

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We investigated the nature of signal recognition, transport, and secretion of mutant hemagglutinins (HAs) of a human influenza virus by the yeast Saccharomyces cerevisiae. The cDNA sequences encoding variant forms of influenza HA were expressed in S. cerevisiae. The HA polypeptides (HA500 and HA325) that were synthesized with their N-terminal signal peptides were correctly targeted to the membrane compartment where they were glycosylated. In contrast, the HA polypeptides (HA484 and HA308) lacking the signal peptide were expressed in the cytoplasm and did not undergo any glycosidic modification, demonstrating the importance of the heterologous signal sequence in the early steps of translocation in S. cerevisiae. The analysis of the N-terminal amino acid sequence of HA500 and HA325 polypeptides demonstrated the correct cleavage of the signal peptide, indicating the structural compatibility of a heterologous signal peptide for efficient recognition and processing by the yeast translocation machinery. The membrane-sequestered and glycosylated HA polypeptides were relatively stable in S. cerevisiae compared with the signal-minus, nonglycosylated HA molecules. Although both the anchor-minus HA (HA500) and HA1 (HA325) polypeptides were targeted efficiently to the membrane, their glycosylation and transport patterns were shown to be different. During pulse-chase, the HA500 remained cell-associated with no detectable secretion into the extracellular medium, whereas the HA325 secreted into the medium. Furthermore, only the cell-associated and secreted forms of HA325 and not HA500 appeared to have undergone hyperglycosylation with the extensive addition of high-molecular-weight outer-chain mannans. Possible reasons for the observed phenotypic behavior of these two mutant HAs are discussed.
机译：我们调查了信号的识别，运输和人类酵母病毒的突变酵母血凝素（HAs）的酿酒酵母的性质。在酿酒酵母中表达编码流感HA的变体形式的cDNA序列。用其N端信号肽合成的HA多肽（HA500和HA325）正确地靶向了膜腔，在该腔中糖基化。相反，缺乏信号肽的HA多肽（HA484和HA308）在细胞质中表达，并且未进行任何糖苷修饰，证明了异源信号序列在酿酒酵母易位的早期步骤中的重要性。 HA500和HA325多肽的N端氨基酸序列分析表明，该信号肽正确切割，表明异源信号肽的结构相容性，可通过酵母易位机制进行有效识别和加工。与信号减负的非糖基化的HA分子相比，膜分离的和糖基化的HA多肽在酿酒酵母中相对稳定。尽管锚定负号HA（HA500）和HA1（HA325）多肽均有效地靶向了膜，但它们的糖基化和转运模式却有所不同。在脉冲追踪期间，HA500保持与细胞相关，没有可检测到的分泌到细胞外培养基中，而HA325分泌到培养基中。此外，随着大量添加高分子量外链甘露聚糖，只有细胞结合和分泌形式的HA325而非HA500似乎发生了高糖基化。讨论了观察到这两个突变型HA的表型行为的可能原因。

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