The structure of human rhinovirus 16

Oliveira, Marcos Antônio de; Zhao, Rui; Lee, Wai-Ming; Kremer, Marcia J.; Minor, Iwona; Rueckert, Roland R.; Diana, Guy D.; Pevear, Daniel C.; Dutko, Frank J.; McKinlay, Mark A.; Rossmann, Michael G.

doi:10.1016/0969-2126(93)90008-5

Cited by 155 publications

(193 citation statements)

References 64 publications

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“…Alternatively, Fab-virus interactions might facilitate the binding of this small compound but, because conformational changes do not occur at the contact interfaces upon Fab binding, it is unlikely that the canyon floor would be affected by Fab binding. Nevertheless, the appearance of this density raises the possibility that previously observed 'pocket factors' 10 , which bind to the same site on other serotypes of HRV and give a nearly identical appearance, may have come from the crystallization mother liquor rather than from the host cell.…”

mentioning

confidence: 84%

Neutralizing antibody to human rhinovirus 14 penetrates the receptor-binding canyon

Smith

Chase

Schmidt

et al. 1996

Nature

181

149

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The three-dimensional structure of intact human rhinovirus 14 (HRV-14) complexed with Fab fragments (Fab17-IA) from a strongly neutralizing antibody that binds bivalently to the virion 1,2 has been determined to 4.0 Å resolution by a combination of X-ray crystallography and cryoelectron microscopy. In contradiction to the most commonly held model of antibody-mediated neutralization, Fab17-IA does not induce a conformational change in the HRV-14 capsid. Instead, the paratope of the antibody undergoes a large conformational change to accommodate the epitope. Unlike any previously described antibody-antigen structure, the conserved framework region of the antibody makes extensive contact with the viral surface. Fab17-IA penetrates deep within the canyon in which the cellular receptor for HRV-14 binds 3,4 . Hence, it is unlikely that viral quaternary structure evolves merely to evade immune recognition. Instead, the shape and position of the receptor-binding region on a virus probably dictates receptor binding and subsequent uncoating events and has little or no influence on concealing the virus from the immune system.The capsid of HRV-14 is composed of 60 copies of four viral proteins, VP1-VP4. Each of the first three proteins has a relative molecular mass of ~30,000 (M r ~ 30K) and a similar ²-barrel structure. The smaller VP4 (M r ~ 7K) lies at the capsid-RNA interface with an extended structure 3 . The monoclonal antibody 17-IA binds to the NIm-IA site which was defined by natural escape mutations at residues D1091 and E1095 on the B-C loop of VP1 (the first digit designates the viral protein and the remaining three designate the residue number). The NIm-IA epitope lies at the 'north rim' of a depression (canyon) on the viral surface that encircles each of the five-fold icosahedral axes of the virus 3 and is where the receptor, ICAM-1, binds 4 . The variable domains (V H · V L ) of Fab17-IA make extensive contact with both the north and south walls of the canyon region. At the north wall, the antigen-binding region (paratope) contacts ~550 Å 2 of the viral surface around NIm-IA site (Fig. 1). The heavychain hypervariable region dominates the contact surface: 23 residues from the heavy chain but only 9 residues from the light chain. As was proposed on the basis of cryo-electron microscopy on this HRV/Fab complex 5 , coulombic interactions dominate the paratopeepitope interface with roughly two-thirds of the total buried viral surface being contributed CORRESPONDENCE and requests for materials should be addressed to H.R.B. (hbourne@quickmail.ucsf.edu). Although somatic mutations occur throughout the variable domain 7 , it is unlikely that mutations in these framework sites that contact the viral surface are merely coincidental. NIH Public AccessSeveral large changes in the Fab17-IA structure accompany binding to HRV-14, although the virus capsid remains essentially rigid (Fig. 2a). A large conformational change occurs in the heavy-chain CDR3 loop (Fig. 2b, c, d) where the Cα atom of Tyr102 H moves up to 5...

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mentioning

confidence: 84%

Neutralizing antibody to human rhinovirus 14 penetrates the receptor-binding canyon

Smith

Chase

Schmidt

et al. 1996

Nature

181

149

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“…Since then, structures of several other picornaviruses have been described (1,34,35,41,48,56,62,(65)(66)(67)84,85,104,112,121,122). The protein shell of the virion is composed of 60 copies of the 4 capsid proteins, VP1, VP2, VP3, and VP4, that are arranged on an icosahedral surface.…”

Section: The Virionmentioning

confidence: 99%

Poliovirus Cell Entry: Common Structural Themes in Viral Cell Entry Pathways

Hogle

2002

Annu. Rev. Microbiol.

312

305

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Structural studies of polio-and closely related viruses have provided a series of snapshots along their cell entry pathways. Based on the structures and related kinetic, biochemical, and genetic studies, we have proposed a model for the cell entry pathway for polio-and closely related viruses. In this model a maturation cleavage of a capsid protein precursor locks the virus in a metastable state, and the receptor acts like a transition-state catalyst to overcome an energy barrier and release the mature virion from the metastable state. This initiates a series of conformational changes that allow the virus to attach to membranes, form a pore, and finally release its RNA genome into the cytoplasm. This model has striking parallels with emerging models for the maturation and cell entry of more complex enveloped viruses such as influenza virus and HIV.

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“…5c3 and 5d3) with a low-resolution representation of the HRV16 atomic structure ( Fig. 5c1; Oliveria et al, 1993) shows that HRV16 reconstructions indeed show very subtle yet genuine features that distinguish the two HRV serotypes. For example, a ridge of density in HRV16 that crosses the ''canyon'' surrounding the star-shaped pentamers (Fig.…”

Section: Example 4: Hrv14 and Hrv16 Models-analysis Of Hrv16mentioning

confidence: 99%