| 论文题目: | N-glycosylation of Gel1 or Gel2 is vital for cell wall β-glucan synthesis in Aspergillus fumigatus |
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| 作者: | Zhao Wan, Lü Yang, Ouyang Haomiao, Zhou Hui, Yan Jianghong, Du Ting, Jin Cheng |
| 联系作者: | Jin Cheng |
| 刊物名称: | Glycobiology |
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| 年份: | 2013 |
| 影响因子: | 4.044 |
| 论文下载: | 下载地址 |
| 摘要: | Fungal cell wall is a dynamic structure that communicates with and protects the cell from the outside stress. In Aspergillus fumigatus, the cell wall β-glucans are mainly elongated by β-1,3-glucanosyltransferases Gels, which consist of seven family members (Gel1-7) utilizing β-1,3-glucan chains as substrates. Previously, we have shown that mutant deficient of N-glycan processing displays a reduction of the cell wall β-glucans, suggesting that N-glycosylation is required for proper function of β-1,3-glucanosyltransferase. To verify this hypothesis, in this study the gene encoding β-1,3-glucanosyltransferase Gel1 or Gel2 was deleted in the Δcwh41 mutant to construct a double-mutant Δgel1Δcwh41 or Δgel2Δcwh41. The growth phenotypes of both double mutants were similar to the single-mutant Δcwh41, suggesting that Gel1 and Gel2 are proteins those are mainly affected by deficient N-glycan processing in the Δcwh41. Furthermore, the mutant Δgel1Gel1-NM or Δgel2Gel2-NM, in which all potential N-glycosylation sites on Gel1 or Gel2 were removed by site-directed mutagenesis, showed phenotypes similar to the single-mutant Δgel1 or Δgel2. Biochemical analysis revealed that N-glycosylation was essential for function of Gel1 or Gel2, and thus required for β-glucan synthesis in A. fumigatus. |
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