Class IIC α-mannosidase AfAms1 is required for morphogenesis and cellular function in Aspergillus fumigatus

نویسندگان

  • Yanjie Li
  • Wenxia Fang
  • Lei Zhang
  • Haomiao Ouyang
  • Hui Zhou
  • Yuanming Luo
  • Cheng Jin
چکیده

The mammalian ER/cytosolic α-mannosidase (Man2C1p), yeast vacuolar α-mannosidase (Ams1p) and the Aspergillus nidulans α-mannosidase are members of Class IIC subgroup, which is involved in oligosaccharide catabolism and N-glycan processing. Unlike their mammalian counterparts, the yeast Ams1p and A. nidulans Class IIC α-mannosidase are not essential for morphogenesis and cellular function. In this study, the Afams1, a gene encoding a member of Class IIC α-mannosidases, was identified in the opportunistic pathogen Aspergillus fumigatus. Deletion of the Afams1 led to a severe defect in conidial formation, especially at a higher temperature. In addition, abnormalities of polarity and septation were associated with the Afams1 mutant. Our results showed that the Afams1 gene, in contrast to its homolog in yeast or A. nidulans, was required for morphogenesis and cellular function in A. fumigatus.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Class IIC alpha-mannosidase AfAms1 is required for morphogenesis and cellular function in Aspergillus fumigatus.

The mammalian ER/cytosolic alpha-mannosidase (Man2C1p), yeast vacuolar alpha-mannosidase (Ams1p) and the Aspergillus nidulans alpha-mannosidase are members of Class IIC subgroup, which is involved in oligosaccharide catabolism and N-glycan processing. Unlike their mammalian counterparts, the yeast Ams1p and A. nidulans Class IIC alpha-mannosidase are not essential for morphogenesis and cellular...

متن کامل

Deletion of the msdS/AfmsdC gene induces abnormal polarity and septation in Aspergillus fumigatus.

alpha-Mannosidases play an important role in the processing of mannose-containing glycans in eukaryotes. A deficiency in alpha-mannosidase is lethal in humans and cattle. In contrast to mammals, Saccharomyces cerevisiae does not require the endoplasmic reticulum alpha-mannosidase gene for growth. However, little is known of the consequence of loss of function of class I alpha-mannosidases in fi...

متن کامل

Differential Support of Aspergillus fumigatus Morphogenesis by Yeast and Human Actins

The actin cytoskeleton is highly conserved among eukaryotes and is essential for cellular processes regulating growth and differentiation. In fungi, filamentous actin (F-actin) orchestrates hyphal tip structure and extension via organization of exocytic and endocytic processes at the hyphal tip. Although highly conserved, there are key differences among actins of fungal species as well as betwe...

متن کامل

β-1,3-glucan modifying enzymes in Aspergillus fumigatus

In Aspergillus fumigatus like in other filamentous ascomycetes, β-1,3-glucan constitutes a prominent cell wall component being responsible for rigidity of the cell wall structure. In filamentous fungi, softening of the cell wall is absolutely required during conidial germination and hyphal branching. Because of the central structure of β-1,3-glucans, it is expected that β-1,3-glucanases play a ...

متن کامل

Significant structural change in both O- and N-linked carbohydrate moieties of the antigenic galactomannan from Aspergillus fumigatus grown under different culture conditions.

Invasive aspergillosis is an important cause of morbidity and mortality in immunocompromised patients. Diagnosis of this infection frequently employs detection of the circulating galactomannan in the patient serum using enzyme immunoassay (EIA), a highly sensitive and specific system. Although there are many structural studies of the galactomannan of Aspergillus fumigatus, some inconsistencies ...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:

دوره   شماره 

صفحات  -

تاریخ انتشار 2009