Fourth Human Parechovirus Serotype

Benschop, Kimberley; Schinkel, Janke; Luken, Manon E.; Broek, Peter J.M. van den; Beersma, Matthias F. C.; Menelik, N.; Zaaijer, Hans L.; Vandenbroucke‐Grauls, C. M. J. E.; Beld, Marcel; Wolthers, Katja C.

doi:10.3201/eid1210.051647

Cited by 124 publications

(102 citation statements)

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“…CAV9 interacts with integrins aVb3 and aVb6 via an RGD motif (Roivainen et al, 1991(Roivainen et al, , 1994Williams et al, 2004). Similar functional RGD motifs have been identified in some other picornaviruses such as echovirus 9 Barty strain (an enterovirus; Zimmermann et al, 1997), human parechoviruses 1, 2, 4, 5 and 6 (HPEVs; Hyypiä et al, 1992;Ghazi et al, 1998;Benschop et al, 2006) and foot-and-mouth disease virus (FMDV; Mason et al, 1994). Other suggested receptors with possible roles in post-attachment and/or internalization of CAV9, include GRP78 (Hsp70-5) and b 2 -microglobulin/ major histocompatibility complex I protein(s) (Triantafilou et al, 1999(Triantafilou et al, , 2000a(Triantafilou et al, , 2002.…”

Section: Introductionmentioning

confidence: 86%

Integrin V 6 is a high-affinity receptor for coxsackievirus A9

Heikkilä

Susi

Stanway

et al. 2009

Journal of General Virology

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Coxsackievirus A9 (CAV9), a member of the genus Enterovirus in the family Picornaviridae, possesses an integrin-binding arginine-glycine-aspartic acid (RGD) motif in the C terminus of VP1 capsid protein. CAV9 has been shown to utilize integrins aVb3 and aVb6 as primary receptors for cell attachment. While CAV9 RGD-mutants (RGE and RGDdel) are capable of infecting rhabdomyosarcoma (RD) cell line, they grow very poorly in an epithelial lung carcinoma cell line (A549). In this study, the relationships between CAV9 infectivity in A549 and RD cells, receptor expression and integrin binding were analysed. A549 cells were shown to express both integrins aVb3 and aVb6, whereas aVb6 expression was not detected on the RD cells. Native CAV9 but not RGE and RGDdel mutants bound efficiently to immobilized aVb3 and aVb6. Adhesion of CAV9 but not RGE/RGDdel to A549 cells was also significantly higher than to RD cells. In contrast, no affinity or adhesion of bacterially produced VP1 proteins to the integrins or to the cells was detected. Function-blocking antibodies against aV-integrins blocked CAV9 but not CAV9-RGDdel infectivity, indicating that the viruses use different internalization routes; this may explain the differential infection kinetics of CAV9 and RGDdel. In an affinity assay, soluble aVb6, but not aVb3, bound to immobilized CAV9. Similarly, only soluble aVb6 blocked virus infectivity. These data suggest that CAV9 binding to aVb6 is a high-affinity interaction, which may indicate its importance in clinical infections; this remains to be determined.

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Section: Introductionmentioning

confidence: 86%

Integrin V 6 is a high-affinity receptor for coxsackievirus A9

Heikkilä

Susi

Stanway

et al. 2009

Journal of General Virology

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Section: Introductionmentioning

confidence: 99%

“…Recently, HPeV1 has also been linked to otitis media (Tauriainen et al, 2008). With the isolation of several HPeV types in recent studies AlSunaidi et al, 2007;Baumgarte et al, 2008;Benschop et al, 2006b; Drexler et al, 2009;Ito et al, 2004;Li et al, 2009), eight types (1-8) of HPeVs are currently known.HPeVs have several distinctive features compared with other picornaviruses (Ghazi et al, 1998;Hyypiä et al, 1992;Stanway et al, 1994Stanway et al, , 2000. Post-translational cleavage of the polyprotein results in only three structural proteins (VP0, VP3 and VP1), as the cleavage of VP0 to VP4 and VP2 seen in other picornaviruses does not occur (Stanway et al, 1994).…”

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confidence: 99%

Evolution and conservation in human parechovirus genomes

Williams

Panayiotou

Girling

et al. 2009

Journal of General Virology

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Human parechoviruses (HPeVs) are frequent pathogens with a seroprevalance of over 90 % in adults. Recent studies on these viruses have increased the number of HPeV types to eight. Here we analyse the complete genome of one clinical isolate, PicoBank/HPeV1/a, and VP1 and 3D protein sequences of PicoBank/HPeV6/a, isolated from the same individual 13 months later. PicoBank/HPeV1/a is closely related to other recent HPeV1 isolates but is distinct from the HPeV1 Harris prototype isolated 50 years ago. The availability of an increasing number of HPeV sequences has allowed a detailed analysis of these viruses. The results add weight to the observations that recombination plays a role in the generation of HPeV diversity. An important finding is the presence of unexpected conservation of codons utilized in part of the 3D-encoding region, some of which can be explained by the presence of a phylogenetically conserved predicted secondary structure domain. This suggests that in addition to the cis-acting replication element, RNA secondary structure domains in coding regions play a key role in picornavirus replication. INTRODUCTIONPicornaviruses are non-enveloped, positive-sense RNA viruses with icosahedral capsids, composed of 60 copies of three or four virus-encoded proteins (VP1-4 or VP0, VP1 and VP3) (Stanway et al., 2002(Stanway et al., , 2005. They have a genome of around 7000-8000 nt encoding one polyprotein which is cleaved by virus proteases to give the structural and non-structural (2A-C and 3A-D) proteins. Picornaviruses consist of economically and socially very important human and animal viruses such as polioviruses, other enteroviruses, rhinoviruses, hepatitis A virus, footand-mouth disease virus and parechoviruses. Currently, parechoviruses consist of two species: human parechovirus (HPeV) and Ljungan virus (LV) (Johansson et al., 2002;Joki-Korpela & Hyypiä, 2001;Stanway & Hyypiä, 1999;Stanway et al., 2000). HPeVs are frequent infectious agents and although they usually cause mild gastroenteritis and respiratory disease in young children, more serious cases, such as flaccid paralysis, encephalitis and myocarditis, have also been reported, particularly associated with HPeV3 infection (Baumgarte et al., 2008;Benschop et al., 2006a Benschop et al., , 2008bEhrnst & Eriksson, 1993;Figueroa et al., 1989;Harvala et al., 2008Harvala et al., , 2009Joki-Korpela & Hyypiä, 2001). Recently, HPeV1 has also been linked to otitis media (Tauriainen et al., 2008). With the isolation of several HPeV types in recent studies AlSunaidi et al., 2007;Baumgarte et al., 2008;Benschop et al., 2006b; Drexler et al., 2009;Ito et al., 2004;Li et al., 2009), eight types (1-8) of HPeVs are currently known.HPeVs have several distinctive features compared with other picornaviruses (Ghazi et al., 1998;Hyypiä et al., 1992;Stanway et al., 1994Stanway et al., , 2000. Post-translational cleavage of the polyprotein results in only three structural proteins (VP0, VP3 and VP1), as the cleavage of VP0 to VP4 and VP2 seen in other picornaviruses does n...

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“…HPeV types 1 and 2 had been known as echoviruses 22 and 23 within the genus Enterovirus but were recognized in the early 1990s as an independent genus (2). Recognition of clinical relevance is increasing after 4 novel types were more recently described (3)(4)(5)(6)(7).…”

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confidence: 99%