The Atomic Structure of Mengo Virus at 3.0 Å Resolution
Abstract
The structure of Mengo virus, a representative member of the cardio picornaviruses, is substantially different from the structures of rhino- and polioviruses. The structure of Mengo virus was solved with the use of human rhinovirus 14 as an 8 Å resolution structural approximation. Phase information was then extended to 3 Å resolution by use of the icosahedral symmetry. This procedure gives promise that many other virus structures also can be determined without the use of the isomorphous replacement technique. Although the organization of the major capsid proteins VP1, VP2, and VP3 of Mengo virus is essentially the same as in rhino- and polioviruses, large insertions and deletions, mostly in VP1, radically alter the surface features. In particular, the putative receptor binding "canyon" of human rhinovirus 14 becomes a deep "pit" in Mengo virus because of polypeptide insertions in VP1 that fill part of the canyon. The minor capsid peptide, VP4, is completely internal in Mengo virus, but its association with the other capsid proteins is substantially different from that in rhino- or poliovirus. However, its carboxyl terminus is located at a position similar to that in human rhinovirus 14 and poliovirus, suggesting the same autocatalytic cleavage of VP0 to VP4 and VP2 takes place during assembly in all these picornaviruses.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Thirteen neutralization escape mutations mapped to four main antigenic sites that are surface-exposed on the capsid: the VP2 "puff" region, the VP3 "knob" region, a VP1 loop between β-strands B and C (BC loop), and two loops in close proximity to the BC loop denoted VP1 loops I and II.
“Thirteen neutralization escape mutations (shown as green triangles in Fig 8B) mapped to four main antigenic sites that are surface-exposed on the capsid: (i) VP2 “puff” region, (ii) VP3 “knob” region, (iii) a VP1 loop located between β-strands B and C (termed BC loop), and (iv) two loops that are in close proximity to the BC loop denoted VP1 loops I and II [3,68] (Fig 8C).”
Cites
The Anatomy and Taxonomy of Protein Structure
Richardson, J. S. (1981) · Advances in protein chemistry · doi:10.1016/s0065-3233(08)60520-3 · Cited by 3,378 · see citing works
Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 Å resolution
Wilson, I. A., Skehel, J. J., & Wiley, D. C. (1981) · Nature · doi:10.1038/289366a0 · Cited by 2,535 · see citing works
Physical Principles in the Construction of Regular VirusesPreprint
Caspar, D. L. D., & Klug, A. (1962) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.1962.027.001.005 · Cited by 2,524 · see citing works
A graphics model building and refinement system for macromolecules
Jones, T. A. (1978) · Journal of Applied Crystallography · doi:10.1107/s0021889878013308 · Cited by 1,848 · see citing works
Chemical and biological evolution of a nucleotide-binding protein
Rossmann, M. G., Moras, D., & Olsen, K. W. (1974) · Nature · doi:10.1038/250194a0 · Cited by 1,474 · see citing works
Self-citationStructure of a human common cold virus and functional relationship to other picornaviruses
Rossmann, M. G., Arnold, E., Erickson, J. W., Frankenberger, E. A., Griffith, J. P., Hecht, H., Johnson, J. E., Kamer, G., Luo, M., Mosser, A. G., et al. (1985) · Nature · doi:10.1038/317145a0 · Cited by 1,427 · see citing works
Self-citationThree-Dimensional Structure of Poliovirus at 2.9 Å Resolution
Hogle, J. M., Chow, M., & Filman, D. J. (1985) · Science · doi:10.1126/science.2994218 · Cited by 1,262 · see citing works
Comparison of super-secondary structures in proteins
Rao, S. T., & Rossmann, M. G. (1973) · Journal of Molecular Biology · doi:10.1016/0022-2836(73)90388-4 · Cited by 899 · see citing works
Self-citationThe detection of sub-units within the crystallographic asymmetric unit
Rossmann, M. G., & Blow, D. M. (1962) · Acta Crystallographica · doi:10.1107/s0365110x62000067 · Cited by 874 · see citing works
Self-citationTomato bushy stunt virus at 2.9 Å resolution
Harrison, S. C., Olson, A. J., Schutt, C. E., Winkler, F. K., & Bricogne, G. (1978) · Nature · doi:10.1038/276368a0 · Cited by 674 · see citing works
The Site of Attachment in Human Rhinovirus 14 for Antiviral Agents That Inhibit Uncoating
Smith, T. J., Kremer, M. J., Luo, M., et al. (1986) · Science · doi:10.1126/science.3018924 · Cited by 456 · see citing works
Self-citationStructure of southern bean mosaic virus at 2.8 Å resolution
Abad‐Zapatero, C., Abdel‐Meguid, S. S., Johnson, J. E., et al. (1980) · Nature · doi:10.1038/286033a0 · Cited by 375 · see citing works
Location and Characterization of the Antigenic Portion of the FMDV Immunizing Protein
Strohmaier, K., Franze, R., & Adam, K. ‐. (1982) · Journal of General Virology · doi:10.1099/0022-1317-59-2-295 · Cited by 367 · see citing works
3.2 Å structure of the copper-containing, oxygen-carrying protein Panulirus interruptus haemocyanin
Gaykema, W. P. J., Hol, W. G. J., Vereijken, J. M., et al. (1984) · Nature · doi:10.1038/309023a0 · Cited by 332 · see citing works
Polyoma virus capsid structure at 22.5 Å resolution
Rayment, I., Baker, T. S., Caspar, D. L. D., et al. (1982) · Nature · doi:10.1038/295110a0 · Cited by 320 · see citing works
Sherry, B., Mosser, A. G., Colonno, R. J., & Rueckert, R. R. (1986) · Journal of Virology · doi:10.1128/jvi.57.1.246-257.1986 · Cited by 299 · see citing works
Exploring structural homology of proteins
Rossmann, M. G., & Argos, P. (1976) · Journal of Molecular Biology · doi:10.1016/0022-2836(76)90195-9 · Cited by 286 · see citing works
Self-citationThree-Dimensional Structure of the Adenovirus Major Coat Protein Hexon
Roberts, M. M., White, J. L., Grütter, M. G., & Burnett, R. M. (1986) · Science · doi:10.1126/science.3704642 · Cited by 247 · see citing works
A comparison of the heme binding pocket in globins and cytochrome b5.
Rossmann, M. G., & Argos, P. (1975) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)40974-5 · Cited by 236 · see citing works
Self-citationPalmenberg, A. C., Kirby, E. M., Janda, M., Drake, N. L., Duke, G. M., Potratz, K. F., & Collett, M. S. (1984) · Nucleic Acids Research · doi:10.1093/nar/12.6.2969 · Cited by 233 · see citing works
Self-citationGeometric sources of redundancy in intensity data and their use for phase determination
Bricogne, G. (1974) · Acta Crystallographica Section A · doi:10.1107/s0567739474010722 · Cited by 192 · see citing works
Implications of the picornavirus capsid structure for polyprotein processing.
Arnold, E., Luo, M., Vriend, G., Rossmann, M. G., Palmenberg, A. C., Parks, G. D., Nicklin, M. J. H., & Wimmer, E. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.1.21 · Cited by 188 · see citing works
Self-citationEvidence for at least two dominant neutralization antigens on human rhinovirus 14
Sherry, B., & Rueckert, R. R. (1985) · Journal of Virology · doi:10.1128/jvi.53.1.137-143.1985 · Cited by 181 · see citing works
Isolation of a monoclonal antibody that blocks attachment of the major group of human rhinoviruses
Colonno, R. J., Callahan, P. L., & Long, W. J. (1986) · Journal of Virology · doi:10.1128/jvi.57.1.7-12.1986 · Cited by 165 · see citing works
Structural comparisons of some small spherical plant viruses
Rossmann, M. G., Abad‐Zapatero, C., Murthy, M. R. N., et al. (1983) · Journal of Molecular Biology · doi:10.1016/s0022-2836(83)80276-9 · Cited by 103 · see citing works
Self-citationBaxt, B., Morgan, D. O., Robertson, B. H., & Timpone, C. A. (1984) · Journal of Virology · doi:10.1128/jvi.51.2.298-305.1984 · Cited by 97 · see citing works
Comparison of protein structures
Matthews, B. W., & Rossmann, M. G. (1985) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(85)15029-9 · Cited by 94 · see citing works
Self-citationMonoclonal antibodies which block cellular receptors of poliovirus
Minor, P. D., Pipkin, P. A., HOCKLEY, D. J., et al. (1984) · Virus Research · doi:10.1016/0168-1702(84)90039-x · Cited by 90 · see citing works
Purification of a HeLa cell receptor protein for group B coxsackieviruses
Mapoles, J. E., Krah, D., & Crowell, R. L. (1985) · Journal of Virology · doi:10.1128/jvi.55.3.560-566.1985 · Cited by 90 · see citing works
Isolation of a receptor protein involved in attachment of human rhinoviruses
Tomassini, J. E., & Colonno, R. J. (1986) · Journal of Virology · doi:10.1128/jvi.58.2.290-295.1986 · Cited by 75 · see citing works
Lonberg-Holm, K. K., & Butterworth, B. E. (1976) · Virology · doi:10.1016/0042-6822(76)90106-9 · Cited by 64 · see citing works
Ellem, K. A. O., & Colter, J. S. (1961) · Virology · doi:10.1016/0042-6822(61)90365-8 · Cited by 53 · see citing works
Lund, G. A., Ziola, B. R., Salmi, A. A., et al. (1977) · Virology · doi:10.1016/0042-6822(77)90076-9 · Cited by 50 · see citing works
The structure of southern bean mosaic virus at 5 Å resolution
Suck, D., Rayment, I., Johnson, J. E., et al. (1978) · Virology · doi:10.1016/0042-6822(78)90423-3 · Cited by 47 · see citing works
Evidence for a Group Protein in Foot-and-Mouth Disease Virus Particles
Talbot, P. J., Rowlands, D. J., Burroughs, J. N., et al. (1973) · Journal of General Virology · doi:10.1099/0022-1317-19-3-369 · Cited by 44 · see citing works
Physico-chemical studies of three variants of Mengo virus and their constituent ribonućleates
Scraba, D. G., Kay, C. M., & Colter, J. S. (1967) · Journal of Molecular Biology · doi:10.1016/0022-2836(67)90261-6 · Cited by 42 · see citing works
Self-citationA structural comparison of concanavalin a and tomato bushy stunt virus protein
Argos, P., Tsukihara, T., & Rossmann, M. G. (1980) · Journal of Molecular Evolution · doi:10.1007/bf01732946 · Cited by 38 · see citing works
Self-citationZiola, B. R., & Scraba, D. G. (1975) · Virology · doi:10.1016/0042-6822(75)90094-x · Cited by 36 · see citing works
Self-citationEffect of Enzymes on the Attachment of Influenza and Encephalomyocarditis Viruses to Erythrocytes
Burness, A. T. H., & Pardoe, I. U. (1981) · Journal of General Virology · doi:10.1099/0022-1317-55-2-275 · Cited by 33 · see citing works
Ziola, B. R., & Scraba, D. G. (1976) · Virology · doi:10.1016/0042-6822(76)90098-2 · Cited by 32 · see citing works
Self-citationGenomic and receptor attachment differences between Mengovirus and encephalomyocarditis virus
Morishima, T., McClintock, P. R., Aulakh, G. S., et al. (1982) · Virology · doi:10.1016/0042-6822(82)90245-8 · Cited by 32 · see citing works
Hordern, J., Leonard, J. D., & Scraba, D. G. (1979) · Virology · doi:10.1016/0042-6822(79)90379-9 · Cited by 31 · see citing works
Self-citationStudies of the pH inactivation of three variants of Mengo encephalomyelitis virus
Mak, T. W., O’Callaghan, D. J., & Colter, J. S. (1970) · Virology · doi:10.1016/0042-6822(70)90200-x · Cited by 31 · see citing works
Arnold, E., & Rossmann, M. G. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.15.5489 · Cited by 31 · see citing works
Self-citationThe structure of Southern bean mosaic virus at 22.5 Å resolution
Johnson, J. E., Akimoto, T., Suck, D., et al. (1976) · Virology · doi:10.1016/0042-6822(76)90038-6 · Cited by 31 · see citing works
An application of the molecular replacement technique in direct space to a known protein structure
Argos, P., Ford, G. C., & Rossmann, M. G. (1975) · Acta Crystallographica Section A · doi:10.1107/s0567739475001076 · Cited by 29 · see citing works
Self-citationKrah, D., & Crowell, R. L. (1985) · Journal of Virology · doi:10.1128/jvi.53.3.867-870.1985 · Cited by 28 · see citing works
Burness, A. T. H., & Pardoe, I. U. (1983) · Journal of General Virology · doi:10.1099/0022-1317-64-5-1137 · Cited by 27 · see citing works
Mak, T. W., Colter, J. S., & Scraba, D. G. (1974) · Virology · doi:10.1016/0042-6822(74)90193-7 · Cited by 23 · see citing works
Self-citationBoege, U., Ko, D. S., & Scraba, D. G. (1986) · Journal of Virology · doi:10.1128/jvi.57.1.275-284.1986 · Cited by 22 · see citing works
Self-citationNitayaphan, S., Omilianowski, D. R., Tóth, M., et al. (1986) · Intervirology · doi:10.1159/000149693 · Cited by 21 · see citing works
The Surface Nature of Proteins of a Bovine Enterovirus, Before and After Neutralization
Carthew, P. (1976) · Journal of General Virology · doi:10.1099/0022-1317-32-1-17 · Cited by 18 · see citing works
Rayment, I., Baker, T. S., & Caspar, D. L. D. (1983) · Acta Crystallographica Section B Structural Science · doi:10.1107/s0108768183002785 · Cited by 11 · see citing works
Picornaviruses of two different genera have similar structures
Luo, M., Arnold, E., Erickson, J. W., et al. (1984) · Journal of Molecular Biology · doi:10.1016/0022-2836(84)90033-0 · Cited by 5 · see citing works
Self-citationStructure of the mengo virion. V11. Crystallization and preliminary X-ray diffraction analysis
Boege, U., Scraba, D. G., Hayakawa, K., et al. (1984) · Virology · doi:10.1016/0042-6822(84)90156-9 · Cited by 3 · see citing works
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
A cell adhesion molecule, ICAM-1, is the major surface receptor for rhinoviruses
Staunton, D. E., Merluzzi, V. J., Rothlein, R., Barton, R., Marlin, S. D., & Springer, T. A. (1989) · Cell · doi:10.1016/0092-8674(89)90689-2 · Cited by 821 · see citing works
The three-dimensional structure of the bacterial virus MS2
Valegård, K., Liljas, L., Fridborg, K., & Unge, T. (1990) · Nature · doi:10.1038/345036a0 · Cited by 411 · see citing works
The encephalomyocarditis virus
Carocci, M., & Bakkali-Kassimi, L. (2012) · Virulence · doi:10.4161/viru.20573 · Cited by 231 · see citing works
Three-dimensional structure of poliovirus serotype 1 neutralizing determinants
Page, G. S., Mosser, A. G., Hogle, J. M., Filman, D. J., Rueckert, R. R., & Chow, M. (1988) · Journal of Virology · doi:10.1128/jvi.62.5.1781-1794.1988 · Cited by 222 · see citing works
Rhee, S. S., & Hunter, E. (1990) · Cell · doi:10.1016/0092-8674(90)90289-q · Cited by 160 · see citing works
VCAM-1 is a receptor for encephalomyocarditis virus on murine vascular endothelial cells
Huber, S. A. (1994) · Journal of Virology · doi:10.1128/jvi.68.6.3453-3458.1994 · Cited by 88 · see citing works
Structural refinement and analysis of Mengo virus
Krishnaswamy, S., & Rossmann, M. G. (1990) · Journal of Molecular Biology · doi:10.1016/0022-2836(90)90077-y · Cited by 64 · see citing works
Self-citationIsolation and molecular characterization of a second serotype of the encephalomyocarditis virus
Philipps, A., Dauber, M., Groth, M., Schirrmeier, H., Platzer, M., Krumbholz, A., Wutzler, P., & Zell, R. (2012) · Veterinary Microbiology · doi:10.1016/j.vetmic.2012.07.006 · Cited by 33 · see citing works
A highly divergent Encephalomyocarditis virus isolated from nonhuman primates in Singapore
Yeo, D. S.-Y., Lian, J. E., Fernandez, C. J., Lin, Y.-N., Liaw, J. C.-W., Soh, M.-L., Lim, E. A.-S., Chan, K.-P., Ng, M.-L., Tan, H.-C., et al. (2013) · Virology Journal · doi:10.1186/1743-422x-10-248 · Cited by 31 · see citing works
Functional aspects of the capsid structure of mengo virus
Scraba, D. G. (1990) · Journal of Structural Biology · doi:10.1016/1047-8477(90)90057-j · Cited by 11 · see citing works
Self-citationAdhikari, A., Feng, K. H., Shrestha, A., Rodriguez, C. E., Nolan, E. C., Pye, G. W., Gauger, P. C., Denagamage, T., Holmes, E. C., & Allison, A. B. (2026) · PLOS Pathogens · doi:10.1371/journal.ppat.1013861 · Cited by 1 · see citing works
- Authors
- Luo, M., Vriend, G., Kamer, G., Minor, I., Arnold, E., Rossmann, M. G., Boege, U., Scraba, D. G., Duke, G. M., & Palmenberg, A. C.
- Affiliations
- Purdue University West Lafayette (US)
- Department of Biological Sciences, Purdue University, West Lafayette, IN 47907.
- University of Alberta (CA)
- University of Wisconsin–Madison (US)
- Venue
- Science
- Published
- 1987-01-09
- Volume
- 235
- Issue
- 4785
- Pages
- 182-191
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2002075344
- Cited by
- 357
- References
- 55
- Citations by year
- 2026: 1 · 2025: 2 · 2024: 4 · 2023: 1 · 2022: 3 · 2021: 6 · 2019: 3 · 2018: 5 · 2017: 4 · 2016: 7 · 2015: 7 · 2014: 9 · 2013: 7 · 2012: 4
- FWCI
- 57.35
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Rutgers University Community Repository (Rutgers University) (submittedVersion)
- Topics
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Advanced Electron Microscopy Techniques and Applications
- Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Viral Infections and Immunology Research
- Keywords
- mengovirus, picornavirus, viral capsid structure, VP1, VP2, VP3, VP4, VP0, isomorphous replacement, icosahedral symmetry, viral assembly, autocatalytic cleavage, human rhinovirus 14
- MeSH terms
- Antigens, Viral, Antiviral Agents, Binding Sites, Capsid, Crystallography, Mengovirus, Protein Conformation, Receptors, Virus, Rhinovirus, Poliovirus, Macromolecular Substances
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
