Development of human antibodies against linear antigenic and immunogenic regions of respiratory syncytial virus (RSV) nucleocapsid and phospho-proteins shows the site-directed characteristics

Leonova, Irina V; Leonov, Sergey; Waris, Matti; Russi, José; Grandien, M; Norrby, Erling

doi:10.1016/s1386-6532(98)00045-2

Cited by 3 publications

(2 citation statements)

References 27 publications

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“…The response to the M protein of RSV varied among patients [Gimenez et al, 1987]. Dissimilarity of these immune responses may arise as a result of difference in availability of either antigenic sites or a certain epitope of the protein to immune recognition [Leonova et al, 1998]. …”

Section: Discussionmentioning

confidence: 99%

Detection of antibodies against human metapneumovirus by western blot using recombinant nucleocapsid and matrix proteins

et al. 2006

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Detection of antibodies against individual proteins of human metapneumovirus (hMPV) is important in the analysis of immune responses to hMPV. Specific antibodies against nucleocapsid (N) and matrix (M) proteins in 97 serum samples were tested by Western blot using recombinant N and M proteins of hMPV expressed in Escherichia coli. The results were compared with those of immunofluorescence assays (IFAs) based on hMPV-infected LLC-MK2 cells, which expressed the whole hMPV proteins. Thirty (61.2%) and 31 (63.3%) of 49 serum samples with titers of > or = 1:160 by IFA reacted with N and M proteins, respectively. Only 2 (4.2%) of 11 serum samples with titers of 1:80 by IFA reacted with N and M proteins. Antibodies against N and M proteins were not detected in 37 serum samples with titers of < 1:40 by IFA. These results indicate that the antibodies against N and M proteins are highly specific (100%) but less sensitive (42.1%, N protein; 40.8%, M protein) than those against whole proteins of hMPV detected by IFA. The reactivity of sera with the recombinant N protein and that with the recombinant M protein correlated well (correlation coefficient of 0.79), and the concordance of reactivities was 91% (kappa = 0.79). In summary, both recombinant N and M proteins of hMPV were antigenic, and the responses to N and M protein varied among patients. Therefore, Western blot using N and M proteins provide a useful tool for analysis of immune responses to hMPV.

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Section: Discussionmentioning

confidence: 99%

Detection of antibodies against human metapneumovirus by western blot using recombinant nucleocapsid and matrix proteins

et al. 2006

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“…The remainder of the samples in the panel were obtained between 11 months and 11 years post-infection. It is known that epitope recognition varies with IgM and IgG class switching and with affinity maturation of the IgG response to viral infections [9, 10]. As the majority of the serum samples included in the pools used to screen the peptide library were obtained at least 1 year post-infection, it is possible that the six peptides identified in the initial ELISA screen are better recognized by antibodies in the later convalescent phase when extensive affinity maturation of IgG responses has occurred.…”

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confidence: 99%

Identification of human linear B-cell epitope sites on the envelope glycoproteins of Crimean-Congo haemorrhagic fever virus

2014

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A peptide library was used to screen for regions containing potential linear B-cell epitope sites in the glycoproteins and nucleoprotein of Crimean-Congo haemorrhagic fever virus (CCHFV) in an enzyme-linked immunosorbent assay (ELISA). The library consisted of 156 peptides, spanning the nucleoprotein and mature GN and GC proteins in a 19-mer with 9-mer overlap format. Using pooled serum samples from convalescent patients to screen the library, six peptides were identified as potential epitope sites. Further testing of these six peptides with individual patient sera identified two of these peptides as probable epitope sites, with peptide G1451-1469 reacting to 13/15 and peptide G1613-1631 to 14/15 human sera. These peptides are situated on the GC protein at amino acid positions 1451-1469 (relative to CCHFV isolate SPU103/97) (TCTGCYACSSGISCKVRIH) and 1613-1631 (FMFGWRILFCFKCCRRTRG). Identified peptides may have application in ELISA for diagnostic or serosurveillance purposes.

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Disordered epitopes as peptide vaccines

et al. 2018

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The development of clinically useful peptide‐based vaccines remains a long‐standing goal. This review highlights that intrinsically disordered protein antigens, which lack an ordered three‐dimensional structure, represent excellent starting points for the development of such vaccines. Disordered proteins represent an important class of antigen in a wide range of human pathogens, and, contrary to widespread belief, they are frequently targets of protective antibody responses. Importantly, disordered epitopes appear invariably to be linear epitopes, rendering them ideally suited to incorporation into a peptide vaccine. Nonetheless, the conformational properties of disordered antigens, and hence their recognition by antibodies, frequently depend on the interactions they make and the context in which they are presented to the immune system. These effects must be considered in the design of an effective vaccine. Here we discuss these issues and propose design principles that may facilitate the development of peptide vaccines targeting disordered antigens.

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Development of human antibodies against linear antigenic and immunogenic regions of respiratory syncytial virus (RSV) nucleocapsid and phospho-proteins shows the site-directed characteristics

Cited by 3 publications

References 27 publications

Detection of antibodies against human metapneumovirus by western blot using recombinant nucleocapsid and matrix proteins

Detection of antibodies against human metapneumovirus by western blot using recombinant nucleocapsid and matrix proteins

Identification of human linear B-cell epitope sites on the envelope glycoproteins of Crimean-Congo haemorrhagic fever virus

Disordered epitopes as peptide vaccines

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