Defining the filarial N-glycoproteome by glycosite mapping in the human parasitic nematode Brugia malayi
Abstract N-linked glycosylation is a critical post translational modification of eukaryotic proteins. N-linked glycans are present on surface and secreted filarial proteins that play a role in host parasite interactions. Examples of glycosylated Brugia malayi proteins have been previously identified...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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Nature Portfolio
2023-05-01
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| Series: | Scientific Reports |
| Online Access: | https://doi.org/10.1038/s41598-023-34936-9 |
| _version_ | 1797822881416085504 |
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| author | Fana B. Mersha Colleen M. McClung Minyong Chen Cristian I. Ruse Jeremy M. Foster |
| author_facet | Fana B. Mersha Colleen M. McClung Minyong Chen Cristian I. Ruse Jeremy M. Foster |
| author_sort | Fana B. Mersha |
| collection | DOAJ |
| description | Abstract N-linked glycosylation is a critical post translational modification of eukaryotic proteins. N-linked glycans are present on surface and secreted filarial proteins that play a role in host parasite interactions. Examples of glycosylated Brugia malayi proteins have been previously identified but there has not been a systematic study of the N-linked glycoproteome of this or any other filarial parasite. In this study, we applied an enhanced N-glyco FASP protocol using an engineered carbohydrate-binding protein, Fbs1, to enrich N-glycosylated peptides for analysis by LC-MS/MS. We then mapped the N-glycosites on proteins from three host stages of the parasite: adult female, adult male and microfilariae. Fbs1 enrichment of N-glycosylated peptides enhanced the identification of N-glycosites. Our data identified 582 N-linked glycoproteins with 1273 N-glycosites. Gene ontology and cell localization prediction of the identified N-glycoproteins indicated that they were mostly membrane and extracellular proteins. Comparing results from adult female worms, adult male worms, and microfilariae, we find variability in N-glycosylation at the protein level as well as at the individual N-glycosite level. These variations are highlighted in cuticle N-glycoproteins and adult worm restricted N-glycoproteins as examples of proteins at the host parasite interface that are well positioned as potential therapeutic targets or biomarkers. |
| first_indexed | 2024-03-13T10:15:51Z |
| format | Article |
| id | doaj.art-83fcd7ce5c184303a8645057b3b59808 |
| institution | Directory Open Access Journal |
| issn | 2045-2322 |
| language | English |
| last_indexed | 2024-03-13T10:15:51Z |
| publishDate | 2023-05-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Scientific Reports |
| spelling | doaj.art-83fcd7ce5c184303a8645057b3b598082023-05-21T11:14:12ZengNature PortfolioScientific Reports2045-23222023-05-0113111710.1038/s41598-023-34936-9Defining the filarial N-glycoproteome by glycosite mapping in the human parasitic nematode Brugia malayiFana B. Mersha0Colleen M. McClung1Minyong Chen2Cristian I. Ruse3Jeremy M. Foster4New England BiolabsNew England BiolabsNew England BiolabsNew England BiolabsNew England BiolabsAbstract N-linked glycosylation is a critical post translational modification of eukaryotic proteins. N-linked glycans are present on surface and secreted filarial proteins that play a role in host parasite interactions. Examples of glycosylated Brugia malayi proteins have been previously identified but there has not been a systematic study of the N-linked glycoproteome of this or any other filarial parasite. In this study, we applied an enhanced N-glyco FASP protocol using an engineered carbohydrate-binding protein, Fbs1, to enrich N-glycosylated peptides for analysis by LC-MS/MS. We then mapped the N-glycosites on proteins from three host stages of the parasite: adult female, adult male and microfilariae. Fbs1 enrichment of N-glycosylated peptides enhanced the identification of N-glycosites. Our data identified 582 N-linked glycoproteins with 1273 N-glycosites. Gene ontology and cell localization prediction of the identified N-glycoproteins indicated that they were mostly membrane and extracellular proteins. Comparing results from adult female worms, adult male worms, and microfilariae, we find variability in N-glycosylation at the protein level as well as at the individual N-glycosite level. These variations are highlighted in cuticle N-glycoproteins and adult worm restricted N-glycoproteins as examples of proteins at the host parasite interface that are well positioned as potential therapeutic targets or biomarkers.https://doi.org/10.1038/s41598-023-34936-9 |
| spellingShingle | Fana B. Mersha Colleen M. McClung Minyong Chen Cristian I. Ruse Jeremy M. Foster Defining the filarial N-glycoproteome by glycosite mapping in the human parasitic nematode Brugia malayi Scientific Reports |
| title | Defining the filarial N-glycoproteome by glycosite mapping in the human parasitic nematode Brugia malayi |
| title_full | Defining the filarial N-glycoproteome by glycosite mapping in the human parasitic nematode Brugia malayi |
| title_fullStr | Defining the filarial N-glycoproteome by glycosite mapping in the human parasitic nematode Brugia malayi |
| title_full_unstemmed | Defining the filarial N-glycoproteome by glycosite mapping in the human parasitic nematode Brugia malayi |
| title_short | Defining the filarial N-glycoproteome by glycosite mapping in the human parasitic nematode Brugia malayi |
| title_sort | defining the filarial n glycoproteome by glycosite mapping in the human parasitic nematode brugia malayi |
| url | https://doi.org/10.1038/s41598-023-34936-9 |
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