FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2069759146> ?p ?o ?g. }

• W2069759146 endingPage "1234" @default.
• W2069759146 startingPage "1223" @default.
• W2069759146 abstract "Glycosylation plays an essential role in regulating protein function by modulating biological, structural, and therapeutic properties. However, due to its inherent heterogeneity and diversity, the comprehensive analysis of protein glycosylation remains a challenge. As part of our continuing effort in the analysis of glycosylation profiles of recombinant HIV-1 envelope-based immunogens, we evaluated and compared the host-cell specific glycosylation pattern of recombinant HIV-1 surface glycoprotein, gp120, derived from clade C transmitted/founder virus 1086.C expressed in Chinese hamster ovary (CHO) and human embryonic kidney containing T antigen (293T) cell lines. We used an integrated glycopeptide-based mass mapping workflow that includes a partial deglycosylation step described in our previous study with the inclusion of a fragmentation technique, electron transfer dissociation (ETD), to complement collision-induced dissociation. The inclusion of ETD facilitated the analysis by providing additional validation for glycopeptide identification and expanding the identified glycopeptides to include coverage of O-linked glycosylation. The site-specific glycosylation analysis shows that the transmitted/founder 1086.C gp120 expressed in CHO and 293T displayed distinct similarities and differences. For N-linked glycosylation, two sites (N386 and N392) in the V4 region were populated with high mannose glycans in the CHO cell-derived 1086.C gp120, while these sites had a mixture of high mannose and processed glycans in the 293T cell-derived 1086.C gp120. Compositional analysis of O-linked glycans revealed that 293T cell-derived 1086.C gp120 consisted of core 1, 2, and 4 type O-linked glycans, while CHO cell-derived 1086.C exclusively consisted of core 1 type O-linked glycans. Overall, glycosylation site occupancy of the CHO and 293T cell-derived 1086.C gp120 showed a high degree of similarity except for one site at N88 in the C1 region. This site was partially occupied in 293T-gp120 but fully occupied in CHO-gp120. Site-specific glycopeptide analysis of transmitted/founder 1086.C gp120 expressed in CHO cells revealed the presence of phosphorylated glycans, while 293T cell-produced 1086.C gp120 glycans were not phosphorylated. While the influence of phosphorylated glycans on immunogenicity is unclear, distinguishing host-cell specific variations in glycosylation profiles provide insights into the similarity (or difference) in recombinant vaccine products. While these differences had minimal effect on envelope antigenicity, they may be important in considering immunogenicity and functional capacities of recombinant envelope proteins produced in different expression systems." @default.
• W2069759146 created "2016-06-24" @default.
• W2069759146 creator A5023314125 @default.
• W2069759146 creator A5027270152 @default.
• W2069759146 creator A5032122826 @default.
• W2069759146 creator A5034518549 @default.
• W2069759146 creator A5051827275 @default.
• W2069759146 creator A5072903008 @default.
• W2069759146 date "2013-02-20" @default.
• W2069759146 modified "2023-09-25" @default.
• W2069759146 title "Characterization of Host-Cell Line Specific Glycosylation Profiles of Early Transmitted/Founder HIV-1 gp120 Envelope Proteins" @default.
• W2069759146 cites W105132506 @default.
• W2069759146 cites W1508509739 @default.
• W2069759146 cites W1528046172 @default.
• W2069759146 cites W1605749013 @default.
• W2069759146 cites W1605996579 @default.
• W2069759146 cites W1965185630 @default.
• W2069759146 cites W1966617266 @default.
• W2069759146 cites W1968014420 @default.
• W2069759146 cites W1971394565 @default.
• W2069759146 cites W1971622553 @default.
• W2069759146 cites W1974887619 @default.
• W2069759146 cites W1975351631 @default.
• W2069759146 cites W1976273041 @default.
• W2069759146 cites W1989184655 @default.
• W2069759146 cites W1993052631 @default.
• W2069759146 cites W1999536165 @default.
• W2069759146 cites W2000475809 @default.
• W2069759146 cites W2002574877 @default.
• W2069759146 cites W2010927211 @default.
• W2069759146 cites W2011401011 @default.
• W2069759146 cites W2019583094 @default.
• W2069759146 cites W2023758594 @default.
• W2069759146 cites W2024191848 @default.
• W2069759146 cites W2042195196 @default.
• W2069759146 cites W2049324939 @default.
• W2069759146 cites W2050478106 @default.
• W2069759146 cites W2050498215 @default.
• W2069759146 cites W2060507246 @default.
• W2069759146 cites W2065118094 @default.
• W2069759146 cites W2069002537 @default.
• W2069759146 cites W2078125368 @default.
• W2069759146 cites W2078913377 @default.
• W2069759146 cites W2079822165 @default.
• W2069759146 cites W2080487519 @default.
• W2069759146 cites W2083344986 @default.
• W2069759146 cites W2083780169 @default.
• W2069759146 cites W2087859193 @default.
• W2069759146 cites W2089509133 @default.
• W2069759146 cites W2094275181 @default.
• W2069759146 cites W2094406292 @default.
• W2069759146 cites W2095910488 @default.
• W2069759146 cites W2096409198 @default.
• W2069759146 cites W2100196601 @default.
• W2069759146 cites W2102952752 @default.
• W2069759146 cites W2103064512 @default.
• W2069759146 cites W2104655459 @default.
• W2069759146 cites W2105548732 @default.
• W2069759146 cites W2118540273 @default.
• W2069759146 cites W2123817807 @default.
• W2069759146 cites W2124764330 @default.
• W2069759146 cites W2126478035 @default.
• W2069759146 cites W2151805116 @default.
• W2069759146 cites W2152708819 @default.
• W2069759146 cites W68286843 @default.
• W2069759146 doi "https://doi.org/10.1021/pr300870t" @default.
• W2069759146 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3674872" @default.
• W2069759146 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/23339644" @default.
• W2069759146 hasPublicationYear "2013" @default.
• W2069759146 type Work @default.
• W2069759146 sameAs 2069759146 @default.
• W2069759146 citedByCount "101" @default.
• W2069759146 countsByYear W20697591462013 @default.
• W2069759146 countsByYear W20697591462014 @default.
• W2069759146 countsByYear W20697591462015 @default.
• W2069759146 countsByYear W20697591462016 @default.
• W2069759146 countsByYear W20697591462017 @default.
• W2069759146 countsByYear W20697591462018 @default.
• W2069759146 countsByYear W20697591462019 @default.
• W2069759146 countsByYear W20697591462020 @default.
• W2069759146 countsByYear W20697591462021 @default.
• W2069759146 countsByYear W20697591462022 @default.
• W2069759146 countsByYear W20697591462023 @default.
• W2069759146 crossrefType "journal-article" @default.
• W2069759146 hasAuthorship W2069759146A5023314125 @default.
• W2069759146 hasAuthorship W2069759146A5027270152 @default.
• W2069759146 hasAuthorship W2069759146A5032122826 @default.
• W2069759146 hasAuthorship W2069759146A5034518549 @default.
• W2069759146 hasAuthorship W2069759146A5051827275 @default.
• W2069759146 hasAuthorship W2069759146A5072903008 @default.
• W2069759146 hasBestOaLocation W20697591462 @default.
• W2069759146 hasConcept C104317684 @default.
• W2069759146 hasConcept C108625454 @default.
• W2069759146 hasConcept C153911025 @default.
• W2069759146 hasConcept C174510640 @default.
• W2069759146 hasConcept C175656101 @default.
• W2069759146 hasConcept C185592680 @default.
• W2069759146 hasConcept C206212055 @default.

• next