Protection against measles virus encephalitis by monoclonal antibodies binding to a cystine loop domain of the H protein mimicked by peptides which are not recognized by maternal antibodies

Ziegler, Diana L.; Fournier, Phillippe; Berbers, Guy A. H.; Steuer, Heiko; Wiesmüller, Karl‐Heinz; Fleckenstein, Burkhard; Schneider, François; Jung, Günther; King, Chwan-Chuen; Muller, Claude P.

doi:10.1099/0022-1317-77-10-2479

Cited by 62 publications

(54 citation statements)

References 52 publications

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“…According to Liebert et al (10), the major antigenic site of MV-H is located between residues 368 and 396, which corresponds exactly to the large insertion at ␤3L23. It has also been reported that a small cysteine cluster region (Cys-381, Cys-386, and Cys-394) at ␤3L23 of MV was identified as a linear neutralizing and protective epitope (22). We identified the most immunodominant epitope, epitope H at aa 383 to 387, on the same loop in RPV.…”

Section: Discussionmentioning

confidence: 71%

“…The B-cell epitopes on the H protein of MV (MV-H) have been analyzed by several groups by using monoclonal antibodies (MAbs) and synthetic peptides. These studies have revealed that seven neutralizing antigenic sites are mapped on MV-H (3,5,7,(10)(11)(12)22). However, the immunodominant neutralizing epitope on H protein remains unclear, while a major antigenic epitope, recognized by acute postinfection human sera, has been identified using synthetic peptides of MV-F protein (1).…”

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confidence: 99%

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Identification of Immunodominant Neutralizing Epitopes on the Hemagglutinin Protein of Rinderpest Virus

Sugiyama

Ito

Minamoto

et al. 2002

J Virol

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Section: Discussionmentioning

confidence: 71%

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confidence: 99%

Identification of Immunodominant Neutralizing Epitopes on the Hemagglutinin Protein of Rinderpest Virus

Sugiyama

Ito

Minamoto

et al. 2002

J Virol

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“…Given that these epitopes on α-helices (helices A, B, and C on MuV-NH and HNE on measles virus H) apparently are not involved in receptor binding (15,29), Abs against them are likely to neutralize the viruses by mechanisms other than the inhibition of receptor binding. Whereas amino acid residues in the HNE region of measles virus H are highly conserved (28), those of the MuV-HN α-helices exhibit diversity among the different genotypes of MuV (Fig. S7, Right).…”

Section: Discussionmentioning

confidence: 99%

“…Helices A, B, and C correspond to α1, α3, and α4, respectively, in the Newcastle disease virus HN protein (14). Interestingly, the similarly positioned α-helix is known as the hemagglutinin noose epitope (HNE; residues at positions 379-410) in measles virus H (28). Given that these epitopes on α-helices (helices A, B, and C on MuV-NH and HNE on measles virus H) apparently are not involved in receptor binding (15,29), Abs against them are likely to neutralize the viruses by mechanisms other than the inhibition of receptor binding.…”

Section: Discussionmentioning

confidence: 99%

Trisaccharide containing α2,3-linked sialic acid is a receptor for mumps virus

Kubota

Takeuchi

Watanabe

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

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Mumps virus (MuV) remains an important pathogen worldwide, causing epidemic parotitis, orchitis, meningitis, and encephalitis. Here we show that MuV preferentially uses a trisaccharide containing α2,3-linked sialic acid in unbranched sugar chains as a receptor. Crystal structures of the MuV attachment protein hemagglutinin-neuraminidase (MuV-HN) alone and in complex with the α2,3-sialylated trisaccharide revealed that in addition to the interaction between the MuV-HN active site residues and sialic acid, other residues, including an aromatic residue, stabilize the third sugar of the trisaccharide. The importance of the aromatic residue and the third sugar in the MuV-HN−receptor interaction was confirmed by computational energy calculations, isothermal titration calorimetry studies, and glycan-binding assays. Furthermore, MuV-HN was found to bind more efficiently to unbranched α2,3-sialylated sugar chains compared with branched ones. Importantly, the strategically located aromatic residue is conserved among the HN proteins of sialic acid-using paramyxoviruses, and alanine substitution compromised their ability to support cellcell fusion. These results suggest that not only the terminal sialic acid but also the adjacent sugar moiety contribute to receptor function for mumps and these paramyxoviruses. The distribution of structurally different sialylated glycans in tissues and organs may explain in part MuV's distinct tropism to glandular tissues and the central nervous system. In the crystal structure, the epitopes for neutralizing antibodies are located around the α-helices of MuV-HN that are not well conserved in amino acid sequences among different genotypes of MuV. This may explain the fact that MuV reinfection sometimes occurs. structure | entry | receptor | infection | paramyxovirus

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“…They are mainly directed against conformational epitopes of the H protein (Bouche et al, 2002). However, vaccine virus-derived monoclonal antibodies (mAbs) BH6 and BH216 neutralize MeVs of various genotypes efficiently by recognizing the linear haemagglutinin noose epitope (HNE; aa 379-410) (Ertl et al, 2003; Santibanez et al, 2005;Ziegler et al, 1996). The HNE domain contains three cysteine residues (C381, C386 and C394) forming a surface-exposed loop (Ziegler et al, 1996).…”

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confidence: 99%

Measles viruses of genotype H1 evade recognition by vaccine-induced neutralizing antibodies targeting the linear haemagglutinin noose epitope

Finsterbusch

Wolbert

Deitemeier

et al. 2009

Journal of General Virology

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The linear haemagglutinin noose epitope (HNE; aa 379-410) is a protective B-cell epitope and considered to be highly conserved in both the vaccine and the wild-type measles virus (MeV) haemagglutinin (H) proteins. Vaccine virus-derived monoclonal antibodies (mAbs) BH6 and BH216, which target the HNE, neutralized MeVs of genotypes B3, C2, D4, D5, D6, D7 and D8, and the vaccine strain Edmonston Zagreb. In the case of genotype H1, only strain Berlin.DEU/ 44.01 was neutralized by these mAbs, whereas strains Shenyang.CHN/22.99 and Sofia.BGR/ 19.05 were not. The H gene sequences of these two strains showed an exchange of proline 397 (P397) to leucine (L397). Mutated H proteins, with P397 exchanged to L and vice versa, were compared with original H proteins by indirect fluorescence assay. H proteins exhibiting P397 but not those with L397 were recognized by BH6 and BH216. This indicates that L397 leads to the loss of the neutralizing HNE. In contrast, human sera obtained from vaccinees (n510) did not discriminate between genotype H1 variants P397 and L397. This concurs with the epidemiological observation that the live-attenuated vaccine protects against both H1 variants. Furthermore, we demonstrated that MeVs of genotype H1 also lack the neutralizing epitopes defined by the vaccine virus-induced mAbs BH15, BH125 and BH47. The loss of several neutralizing epitopes, as shown for H1 viruses currently circulating endemically in Asia, implies that epitope monitoring should be considered to be included in measles surveillance.

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Protection against measles virus encephalitis by monoclonal antibodies binding to a cystine loop domain of the H protein mimicked by peptides which are not recognized by maternal antibodies

Cited by 62 publications

References 52 publications

Identification of Immunodominant Neutralizing Epitopes on the Hemagglutinin Protein of Rinderpest Virus

Identification of Immunodominant Neutralizing Epitopes on the Hemagglutinin Protein of Rinderpest Virus

Trisaccharide containing α2,3-linked sialic acid is a receptor for mumps virus

Measles viruses of genotype H1 evade recognition by vaccine-induced neutralizing antibodies targeting the linear haemagglutinin noose epitope

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