Site-Specific O-Glycosylation Analysis of SARS-CoV-2 Spike Protein Produced in Insect and Human Cells.
Site-Specific O-Glycosylation Analysis of SARS-CoV-2 Spike Protein Produced in Insect and Human Cells.
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对昆虫和人类细胞中产生的 SARS-CoV-2 刺突蛋白进行位点特异性 O 糖基化分析。
DOI：
10.3390/v13040551
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发表时间：
2021-03-25
期刊：
影响因子：
--
通讯作者：
Wandall HH
中科院分区：
文献类型：
--
作者：
Bagdonaite I;Thompson AJ;Wang X;Søgaard M;Fougeroux C;Frank M;Diedrich JK;Yates JR 3rd;Salanti A;Vakhrushev SY;Paulson JC;Wandall HH
包膜病毒不仅劫持宿主的翻译过程，还劫持其糖基化机制，并在不同程度上覆盖具有耐受性宿主结构的病毒表面蛋白。SARS-CoV-2表面蛋白S在病毒表面以三聚体的形式存在，并被n -连接聚糖的致密屏蔽覆盖，并且有一些o -糖位点的报道。o -甘聚糖的位置受一大家族在细胞和组织中表达变化的起始酶控制，因此很难预测。在这里，我们使用我们完善的o -糖蛋白组学工作流程来绘制3种不同实体的蛋白质s -昆虫细胞或人类细胞产生的外结构域或昆虫细胞衍生的受体结合结构域（RBD）上o -连接糖基化位点的精确位置。共鉴定了25个o -糖位点，在不同细胞来源的两个外结构域具有相似的模式，并且单体RBD具有明显的模式。引人注目的是，25个o -糖位点中有16个位于已知n -糖位点的三个氨基酸内。然而，o -糖基化主要发生在未被n -聚糖占用的肽上，否则总体占用率较低。这表明o -聚糖在免疫屏蔽中可能具有互补功能，而o -糖基化对SARS-CoV-2亚单位疫苗设计的影响可以忽略不计。
Enveloped viruses hijack not only the host translation processes, but also its glycosylation machinery, and to a variable extent cover viral surface proteins with tolerogenic host-like structures. SARS-CoV-2 surface protein S presents as a trimer on the viral surface and is covered by a dense shield of N-linked glycans, and a few O-glycosites have been reported. The location of O-glycans is controlled by a large family of initiating enzymes with variable expression in cells and tissues and hence is difficult to predict. Here, we used our well-established O-glycoproteomic workflows to map the precise positions of O-linked glycosylation sites on three different entities of protein S—insect cell or human cell-produced ectodomains, or insect cell derived receptor binding domain (RBD). In total 25 O-glycosites were identified, with similar patterns in the two ectodomains of different cell origin, and a distinct pattern of the monomeric RBD. Strikingly, 16 out of 25 O-glycosites were located within three amino acids from known N-glycosites. However, O-glycosylation was primarily found on peptides that were unoccupied by N-glycans, and otherwise had low overall occupancy. This suggests possible complementary functions of O-glycans in immune shielding and negligible effects of O-glycosylation on subunit vaccine design for SARS-CoV-2.
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DOI：
10.1016/s0140-6736(20)32661-1
发表时间：
2021-01-09
期刊：
Lancet (London, England)
影响因子：
--
作者：
Voysey M;Clemens SAC;Madhi SA;Weckx LY;Folegatti PM;Aley PK;Angus B;Baillie VL;Barnabas SL;Bhorat QE;Bibi S;Briner C;Cicconi P;Collins AM;Colin-Jones R;Cutland CL;Darton TC;Dheda K;Duncan CJA;Emary KRW;Ewer KJ;Fairlie L;Faust SN;Feng S;Ferreira DM;Finn A;Goodman AL;Green CM;Green CA;Heath PT;Hill C;Hill H;Hirsch I;Hodgson SHC;Izu A;Jackson S;Jenkin D;Joe CCD;Kerridge S;Koen A;Kwatra G;Lazarus R;Lawrie AM;Lelliott A;Libri V;Lillie PJ;Mallory R;Mendes AVA;Milan EP;Minassian AM;McGregor A;Morrison H;Mujadidi YF;Nana A;O'Reilly PJ;Padayachee SD;Pittella A;Plested E;Pollock KM;Ramasamy MN;Rhead S;Schwarzbold AV;Singh N;Smith A;Song R;Snape MD;Sprinz E;Sutherland RK;Tarrant R;Thomson EC;Török ME;Toshner M;Turner DPJ;Vekemans J;Villafana TL;Watson MEE;Williams CJ;Douglas AD;Hill AVS;Lambe T;Gilbert SC;Pollard AJ;Oxford COVID Vaccine Trial Group
通讯作者：
Oxford COVID Vaccine Trial Group
影响因子：
7.8
作者：
Prüβ BM
通讯作者：
Prüβ BM
BNT162B2 mRNA COVID-19疫苗的安全性和功效。
DOI：
10.1056/nejmoa2034577
发表时间：
2020-12-31
期刊：
The New England journal of medicine
影响因子：
--
作者：
Polack FP;Thomas SJ;Kitchin N;Absalon J;Gurtman A;Lockhart S;Perez JL;Pérez Marc G;Moreira ED;Zerbini C;Bailey R;Swanson KA;Roychoudhury S;Koury K;Li P;Kalina WV;Cooper D;Frenck RW Jr;Hammitt LL;Türeci Ö;Nell H;Schaefer A;Ünal S;Tresnan DB;Mather S;Dormitzer PR;Şahin U;Jansen KU;Gruber WC;C4591001 Clinical Trial Group
通讯作者：
C4591001 Clinical Trial Group
影响因子：
16.6
作者：
Cao L;Pauthner M;Andrabi R;Rantalainen K;Berndsen Z;Diedrich JK;Menis S;Sok D;Bastidas R;Park SR;Delahunty CM;He L;Guenaga J;Wyatt RT;Schief WR;Ward AB;Yates JR 3rd;Burton DR;Paulson JC
通讯作者：
Paulson JC
DOI：
10.1002/prot.340230412
发表时间：
1995-12-01
期刊：
PROTEINS-STRUCTURE FUNCTION AND GENETICS
影响因子：
--
作者：
Frishman, D;Argos, P
通讯作者：
Argos, P