Journal of Clinical Virology - Volume 82 - Supplement 1 - September 2016

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S20 Abstracts / Journal of Clinical Virology 82S (2016) S1–S142
Abstract no: 96
Presentation at ESCV 2016: Oral 36
Differences among mumps virus surface
proteins between genotype G and other
genotypes and their potential effect on mumps
virus immunity and pathogenesis
T. Vermeire ∗, S. Gouma , S. Van Gucht ,
L. Martens , V. Hutse , J. Cremer , P. Rota ,
G. Leroux-Roels , M. Koopmans ,
R. Van Binnendijk , E. Vandermarliere
1 WIV-ISP, Belgium
2 RIVM, Belgium
3 VIB-UGent, Belgium
4 CDC, Belgium
5 UGent, Belgium
6 RIVM-Erasmus MC, Belgium
Background: Mumps used to be a mild childhood disease, but
recent outbreaks mainly affected vaccinated young adults. One
hypothesis on the recurrence of mumps suggests that there might
be a mismatch between the surface proteins (fusion protein (F)
and hemagglutinin-neuraminidase (HN)) of the Jeryl Lynn vaccine
strain and the circulating genotype G strains. These surface pro-
teins are important for mumps virus immunity and pathogenesis.
In this study, we therefore compared the variable positions in the
F and HN proteins between the Jeryl Lynn vaccine strain and wild
type mumps virus strains, including genotype G.
Methods: Sequence information of the Jeryl Lynn vaccine strain,
genotype G strains and other wild type strains were collected from
UniProt and from clinical samples collected at the RIVM. HN and
F sequencing of the clinical samples was performed at the RIVM
with six primers as described previously As no protein struc-
tures of the F and HN protein were available for the mumps virus,
we have built homology models of the HN and F protein with the
aid of FoldX. The templates used were 4JF7 and 4GIP, respectively.
We have subsequently used the in-house developed Scop3D tool
to visualize the sequence conservation/variation on both protein
structures
Results: For the F andHNprotein, we found that variations occur
in functional or immunological important regions (known B-cell
epitopes, glycosylation sites, etc.). Differences between the Jeryl
Lynn vaccine strains and genotype G were found in known B-cell
epitopes for both the F and HN protein and in glycosylation sites of
the HN protein. Additionally, the variations in genotype G in these
regions, seem to be very specific, as these variations change only to
a limitednumber of other amino acids. Of special interest is the vari-
ations found in amino acid positions 400–402 and 464–466 of the
HN protein, as these positions are theoretical glycosylation sites.
Conclusion: In this study, we have identified multiple vari-
able sites in the mumps virus surface proteins which could affect
mumps virus immunity and pathogenesis. Difference in functional
or immunological important regions of the proteins, such as known
B-cell epitopes and glycosylation sites, could result in a mismatch
between the Jeryl Lynn vaccine strain and circulating genotype G
strains, as antibodies raised through vaccinationwith the Jeryl Lynn
strain might not be able to neutralize the circulating genotype G
strains. This could possibly contribute to the recurrence of mumps
outbreaks in vaccinated young adults.
Reference
[1] S. Gouma, J. Sane, D. Gijselaar, J. Cremer, S. Hahné, M. Koopmans, et al., Two
major mumps genotype G variants dominated recent mumps outbreaks in the
Netherlands (2009–2012), J. Gen. Virol. 95 (Pt 5) (2014) 1074–1082.
[2] T. Vermeire, S. Vermaere, B. Schepens, X. Saelens, S. Van Gucht, L. Martens, E.
Vandermarliere, Scop3D: three-dimensional visualization of sequence
conservation, Proteomics 15 (8) (2015) 1448–1452.
Abstract no: 350
Presentation at ESCV 2016: Oral 37
Structural basis of Zika virus cross-reactivity
and cross-neutralization with flavivirus
post-infection and post-vaccination sera
Karin Stiasny∗, Iris Medits, Stefan Malafa,
Victoria Bradt, Georgios Tsouchnikas,
Judith H. Aberle, Stephan W. Aberle,
Franz X. Heinz
Department of Virology, Medical University of
Vienna, Austria
The explosive spread of Zika virus to Pacific Islands as well as
South- and Middle America underscores the potential threat of
newly emerging arthropod-borne (ARBO) viruses. The evidence of
transplacental infections and associated malformations of new-
borns (microcephalies) led the WHO to declare a Public Health
Emergency of International Concern on February 1, 2016. At present
it is unclear which factors contributed to this emergence, which
may include mutational adaptations that changed the character of
this virus. In addition, however, there is evidence that pre-existing
flavivirus antibodies may play a role in Zika pathogenesis. This is
especially important in the context of other flaviviruses that co-
circulate in Zika-endemic regions.
We have therefore conducted a systematic analysis of Zika virus
cross-reactivity and cross-neutralization of serum samples from
people after infections with heterologous flaviviruses, including
dengue, West Nile and tick-borne encephalitis (TBE) as well as after
yellow fever, Japanese encephalitis and TBE vaccinations. The data
are presented in the context of amino acid sequence divergence
between flaviviruses and the recently determined atomic structure
of the Zika virus envelope protein E. The implications of these find-
ings for the specific serodiagnosis of different flavivirus infections
will be discussed.