Evolution of Cell Recognition by Viruses: A Source of Biological Novelty with Medical Implications

Baranowski, Éric; Ruiz-Jarabo, Carmen M.; Pariente, Nonia; Verdaguer, N.; Domingo, Esteban

doi:10.1016/s0065-3527(03)62002-6

Cited by 64 publications

(72 citation statements)

References 557 publications

(783 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…This substitution became rapidly dominant in the viral population after the reintroduction of the guinea pig-adapted virus into pigs. These observations illustrate how the appearance of minority variant viruses in an unnatural host can result in the dominance of these viruses on reinfection of the original host species.The high potential for adaptation and rapid evolution that derives from the quasispecies dynamics of RNA virus populations (30, 40) can be reflected in the alteration of cell tropism, host range, and virulence (8,9,30,43,51). Mutant viruses with a modified host range can contribute to the emergence of new animal and human diseases (62).…”

mentioning

confidence: 99%

See 1 more Smart Citation

Guinea Pig-Adapted Foot-and-Mouth Disease Virus with Altered Receptor Recognition Can Productively Infect a Natural Host

Núñez

Molina

Baranowski

et al. 2007

J Virol

Self Cite

View full text Add to dashboard Cite

We report that adaptation to infect the guinea pig did not modify the capacity of foot-and-mouth disease virus (FMDV) to kill suckling mice and to cause an acute and transmissible disease in the pig, an important natural host for this pathogen. Adaptive amino acid replacements (I 248 3T in 2C, Q 44 3R in 3A, and L 147 3P in VP1), selected upon serial passages of a type C FMDV isolated from swine (biological clone C-S8c1) in the guinea pig, were maintained after virus multiplication in swine and suckling mice. However, the adaptive replacement L 147 3P, next to the integrin-binding RGD motif at the GH loop in VP1, abolished growth of the virus in different established cell lines and modified its antigenicity. In contrast, primary bovine thyroid cell cultures could be productively infected by viruses with replacement L 147 3P, and this infection was inhibited by antibodies to ␣v␤6 and by an FMDV-derived RGD-containing peptide, suggesting that integrin ␣v␤6 may be used as a receptor for these mutants in the animal (porcine, guinea pig, and suckling mice) host. Substitution T 248 3N in 2C was not detectable in C-S8c1 but was present in a low proportion of the guinea pig-adapted virus. This substitution became rapidly dominant in the viral population after the reintroduction of the guinea pig-adapted virus into pigs. These observations illustrate how the appearance of minority variant viruses in an unnatural host can result in the dominance of these viruses on reinfection of the original host species.The high potential for adaptation and rapid evolution that derives from the quasispecies dynamics of RNA virus populations (30, 40) can be reflected in the alteration of cell tropism, host range, and virulence (8,9,30,43,51). Mutant viruses with a modified host range can contribute to the emergence of new animal and human diseases (62). On the other hand, adaptation to a new host has been exploited since the beginning of vaccinology to derive attenuated strains with decreased pathogenicity for the original, natural host (18).Foot-and-mouth disease virus (FMDV) belongs to the Picornaviridae family and is the etiological agent of the most important animal disease affecting domestic cloven-hoofed animals and a large variety of wild artiodactyls (for reviews, see references 2, 6, 21, 63, 68, and 74). The virus consists of a nonenveloped particle of icosahedral symmetry containing a positive-sense single-stranded RNA genome of about 8.5 kb. A single open reading frame encodes all of the capsid, as well as a total of nine additional mature, nonstructural (NS) proteins, including two proteases (L and 3C) and an RNA-dependent RNA polymerase (3D) (14,69,73). As shown for a number of different picornaviruses, the mature NS proteins, as well as some of their protein precursors, are involved in multiple functions needed for virus multiplication and the host cell membrane rearrangements associated with viral RNA replication (3,25,35,46,55,60,65,82).FMDV can initiate the infection of cultured cells via different ␣v integrins (␣v␤1,␣v␤...

show abstract

mentioning

confidence: 99%

“…The high potential for adaptation and rapid evolution that derives from the quasispecies dynamics of RNA virus populations (30, 40) can be reflected in the alteration of cell tropism, host range, and virulence (8,9,30,43,51). Mutant viruses with a modified host range can contribute to the emergence of new animal and human diseases (62).…”

mentioning

confidence: 99%

Guinea Pig-Adapted Foot-and-Mouth Disease Virus with Altered Receptor Recognition Can Productively Infect a Natural Host

Núñez

Molina

Baranowski

et al. 2007

J Virol

Self Cite

View full text Add to dashboard Cite

show abstract

“…ATPSβ was therefore reported as an important player in the CHIKV infection of mosquito cells indicative of a "conserved virus-arthropod interaction." Viruses have been reported to variably employ only a single receptor to infect their target cells or exploit several alternative cell surface proteins to initiate their replication in different cell lines or to enter the same cell type [34]. Additionally, viruses have also been reported to require multiple cell surface receptors to enter host cells [35].…”

Section: Discussionmentioning

confidence: 99%

Chikungunya Virus Interacts with Heat Shock Cognate 70 Protein to Facilitate Its Entry into Mosquito Cell Line

et al. 2017

View full text Add to dashboard Cite

Aim: The study was designed to identify putative Chikungunya virus (CHIKV) receptor/s on C6/36 cells that facilitate viral entry. Methods: The virus overlay protein binding assay (VOPBA) was adopted to identify CHIKV-interacting bands present in C6/36 cell membrane and identity of the protein was established by mass spectrometry. The role of this protein as a putative CHIKV receptor on C6/36 cells was confirmed by infection inhibition assay. Cell surface localization of the identified protein was studied by indirect immunofluorescence assay (IFA) on nonpermeabilized cells and by flow cytometry. Interaction between this protein and CHIKV was confirmed by co-immunoprecipation (Co-IP) and Western blotting. The effect of depletion of the identified protein by quercetin was demonstrated by infection inhibition assay. Results: A 70-kDa protein was identified as a CHIKV-interacting protein by VOPBA. MALDI-TOF analysis followed by homology search revealed that this protein could be heat shock cognate 70 (HSC 70). Anti-HSC 70 antibodies blocked CHIKV entry into C6/36 cells in a dose-dependent manner. IFA and flow cytometry analysis demonstrated HSC 70 localization on C6/36 cell surface. Co-IP experiments confirmed the interaction between HSC 70 and CHIKV envelope. Quercetin- and YM-01-treated C6/36 cells exhibited dose-dependent infection inhibition. Conclusion: HSC 70 serves as a putative CHIKV receptor on C6/36 cells.

show abstract

“…Any attempt to prevent viral entry requires precise knowledge about the specific interactions between viral surface proteins and cellular receptors [6]. It is observed that small changes in amino acid composition of the viral surface proteins involved in the recognition process often lead to significant changes in binding specificities, and therefore facilitate the crossing of species barriers [2,4,7,8].…”

Section: Introductionmentioning

confidence: 99%

“…Additionally, host cell tropism fluctuates between members of the same genus and even in isolates of one virus [1,4,8]. Knowledge of the molecular recognition of receptors by viruses at atomic resolution is limited and relies mostly on demanding crystallographic studies.…”

Section: Introductionmentioning

confidence: 99%

Molecular Recognition of Ligands by Native Viruses and Virus-Like Particles as Studied by NMR Experiments

Rademacher¹,

Peters²

2008

Topics in Current Chemistry

View full text Add to dashboard Cite

Viral entry into host cells is a process that in the majority of cases is not understoodin its molecular details. The first step of viral entry is the recognition of cellular receptorson host cells by viruses, and although X-ray crystallography had yielded some spectacular resultsin individual cases, in general there is little data available to unravel the principles of virus-ligandrecognition at atomic resolution. Therefore, new techniques that uncover the molecular details ofthese recognition processes are needed. The investigation of virus-ligand interactions usingligand-based NMR techniques is an emerging field with the potential to substantially contribute toa deeper understanding of the molecular aspects of viral entry into host cells. Here, we givean overview that covers some of the systems studied so far. This comprises native viruses as wellas virus-like particles (VLPs). We will not address studies that have been performed with individualproteins that are not in a native environment. It turns out that STD NMR in particular has a greatpotential to shine light on the viral entry process as this technique requires only very moderateamounts of viruses or VLPs and corresponding ligands. As a further advantage, this approachis also applicable to ligands that bind to viruses with medium to low affinity. Therefore, STD NMRis extremely well suited for development of antiviral entry inhibitors utilizing fragment-based approacheswith low molecular weight compounds.

show abstract

Evolution of Cell Recognition by Viruses: A Source of Biological Novelty with Medical Implications

Cited by 64 publications

References 557 publications

Guinea Pig-Adapted Foot-and-Mouth Disease Virus with Altered Receptor Recognition Can Productively Infect a Natural Host

Guinea Pig-Adapted Foot-and-Mouth Disease Virus with Altered Receptor Recognition Can Productively Infect a Natural Host

Chikungunya Virus Interacts with Heat Shock Cognate 70 Protein to Facilitate Its Entry into Mosquito Cell Line

Molecular Recognition of Ligands by Native Viruses and Virus-Like Particles as Studied by NMR Experiments

Contact Info

Product

Resources

About