panoramaProteomicsDaniela VolkeSevere Acute Respiratory Syndrome Coronavirus 2https://panoramaweb.org/RBD_M_Glyco.urldaniela.volke@bbz.uni-leipzig.deUniversität Leipzig/BBZPanoramaPublicSevere acute respiratory syndrome coronavirus 2 (SARS-CoV-2) can infect human cells by first attaching to the ACE-2 receptor via its receptor-binding domain (RBD) in the spike protein. Here, we report the influence of N-glycosylation sites of the RBD and the membrane (M) protein on IgG antibody binding in serum samples from patients infected with the original SARS-CoV-2 strain in Germany. The RBDs of the wildtype, alpha, beta, gamma, and kappa variants expressed in HEK293S GnTI- cells were all N-glycosylated at Asn331, Asn334, Asn343, and Asn360 or Asn370, whereas the M-protein was glycosylated at Asn5. An ELISA using a coated RBD and probed with anti-RBD IgG antibodies gave a sensitivity of 96.3% and a specificity of 100% for the wildtype RBD, while the sensitivity decreased by 5% to 10% for the variants of concern, essentially in the order of appearance. Deglycosylation of the wildtype RBD strongly reduced antibody recognition by ~20%, considering the mean of the absorbances recorded for the ELISA. This effect was even stronger for the unglycosylated RBD expressed in <i>Escherichia coli</i>, suggesting structural changes affecting epitope recognition. Interestingly, the N-glycosylated M-protein expressed in HEK293S GnTI- cells gave good sensitivity (95%), which also decreased to 65% after deglycosylation, and selectivity (100%). In conclusion, N-glycosylation of the M-protein, the RBD, and most likely the spike protein are important for proper antibody binding and immunological assays, whereas the type of N-glycosylation is less relevant.Influence of Mutations and N-Glycosylation Sites in the Receptor-Binding Domain (RBD) and the Membrane Protein of SARS-CoV-2 Variants of Concern on Antibody Binding in ELISA.Schwarze Mandy M, Volke Daniela D, Rojas Echeverri Juan Camilo JC, Schick Robin R, Lakowa Nicole N, Grünewald Thomas T, Wolf Johannes J, Borte Stephan S, Scholz Markus M, Krizsan Andor A, Hoffmann Ralf RVoltage-gated calcium channel subunit alpha Cav1.3, IgG Antibody, CG17907, BamF, O-linked Glycosylations, 3-mannosylglycoprotein beta-1, BamC, AP-2, Tandem, AP-1, Galactosylation, Blood, alpha-Spe, DELTA AND GAMMA, Galactosylations, 2019 novel coronavirus, RBD, gamma-Ada, protein, Serum, betaTub1, Mass Spectrometry Mass Spectrometry, CG31654, alpha-Spc, IgG4 antibody, Membrane Tissues, l(3)04276, B1t, Gamma 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2-beta-N-acetylglucosaminyltransferase activity, LGMD2C, strain, O linked Glycosylation, Bacillus coli, Protein, whole membrane, betaSpec, UDP-N-acetyl-D-glucosamine:3-(alpha-D-mannosyl)-beta-D-mannosyl-glycoprotein 2-beta-N-acetyl-D-glucosaminyltransferase activity, Determinants, b-Spec, opsonin activity, l(1)G0074, transmembrane, l(1)G0198, D-alphaAda, negatron, CG9113, l(3)87Ed, FCP-B, l(2)46Ce, Wuhan, Membrane, alpha-1 polypeptide, l(2)46Cg, SARS-coronavirus 2, Protein Gene Products, l(2)46CFj, l(2)46CFh, l(3)62Bd, beta-spec, l(2)46CFp, Modern Man, BAM, SCARMD2, 7S Gamma Globulin, Bam, l(2)SH0460, B cell receptor activity, Allerglobuline, alfa-Spec, COVID 19 Virus, Summary, E(eve), Serums, Spec, Field Report, l(2)46CFgfalseAnalysis of N-Glycosylation for SARS-CoV-2 expressed receptor-binding domain VOCs and membrane protein with LC-MS.Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) can infect human cells by first attaching to the ACE-2 receptor via its receptor-binding domain (RBD) in the spike protein. We investigated the influence of N-glycosylation sites of the RBD and the membrane (M) protein on IgG antibody binding in serum samples from patients infected with the original SARS-CoV-2 strain in Germany. The N-glycosylation sites Asn331, Asn334, Asn343, Asn370 and Asn381 of RBDs of the wildtype, alpha, beta, gamma, kappa, and omicron BA.1 variants expressed in HEK293T and HEK293S GnTI- cells , as well as Asn5 for the M-protein were analyzed with tandem mass spectrometry for N-glycosylation.Mon Apr 29 00:00:00 GMT+01:00 2024PXD048930269704938666819