{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Liu Y"],"funding":["Dutch Ministry of Agriculture Nature and Food Quality via the knowledge- and innovation KB37 program 'Healthy and Safe food systems'","National Key Research and Development Plan 'modern food processing and food storage and transportation technology and equipment'","China Scholarship Council","National Key Research and Development Plan ‘modern food processing and food storage and transportation technology and equipment’","Chinese Academic of Agricultural Sciences","Dutch Ministry of Agriculture Nature and Food Quality via the knowledge and innovation of KB37 program ‘Healthy and Safe food systems’"],"pagination":["6386"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10490071"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["28(17)"],"pubmed_abstract":["Glycosylation is an important post-translational modification of proteins, contributing to protein function, stability and subcellular localization. Fungal immunomodulatory proteins (FIPs) are a group of small proteins with notable immunomodulatory activity, some of which are glycoproteins. In this study, the impact of glycosylation on the bioactivity and biochemical characteristics of FIP-nha (from <i>Nectria haematococca</i>) is described. Three rFIP-nha glycan mutants (N5A, N39A, N5+39A) were constructed and expressed in <i>Pichia pastoris</i> to study the functionality of the specific N-glycosylation on amino acid N5 and N39. Their protein characteristics, structure, stability and activity were tested. WT and mutants all formed tetramers, with no obvious difference in crystal structure"],"journal":["Molecules (Basel, Switzerland)"],"pubmed_title":["Glycosylation Contributes to Thermostability and Proteolytic Resistance of rFIP-nha (<i>Nectria haematococca</i>)."],"pmcid":["PMC10490071"],"funding_grant_id":["KB-37-001-007","2017YFD0400204"],"pubmed_authors":["Liu Y","Imam KMSU","Li Z","Xie Y","Wichers H","Zhang H","Du G","Wei X","Bastiaan-Net S","Wang Y","Hoppenbrouwers T"],"additional_accession":[]},"is_claimable":false,"name":"Glycosylation Contributes to Thermostability and Proteolytic Resistance of rFIP-nha (<i>Nectria haematococca</i>).","description":"Glycosylation is an important post-translational modification of proteins, contributing to protein function, stability and subcellular localization. Fungal immunomodulatory proteins (FIPs) are a group of small proteins with notable immunomodulatory activity, some of which are glycoproteins. In this study, the impact of glycosylation on the bioactivity and biochemical characteristics of FIP-nha (from <i>Nectria haematococca</i>) is described. Three rFIP-nha glycan mutants (N5A, N39A, N5+39A) were constructed and expressed in <i>Pichia pastoris</i> to study the functionality of the specific N-glycosylation on amino acid N5 and N39. Their protein characteristics, structure, stability and activity were tested. WT and mutants all formed tetramers, with no obvious difference in crystal structure","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Aug","modification":"2026-04-08T14:25:25.043Z","creation":"2025-04-07T03:33:07.36Z"},"accession":"S-EPMC10490071","cross_references":{"pubmed":["37687215"],"doi":["10.3390/molecules28176386"]}}