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Previous Article | Next Article 
Journal of Virology, March 2001, p. 2444-2451, Vol. 75, No. 5
Department of Biological Sciences, Purdue
University, West Lafayette, Indiana 47907-1392,1
and Department of Molecular Genetics and Microbiology, School
of Medicine, State University of New York, Stony Brook, New York
11794-52222
Received 15 September 2000/Accepted 28 November 2000
Coxsackievirus A21 (CAV21), like human rhinoviruses (HRVs), is a
causative agent of the common cold. It uses the same cellular receptor,
intercellular adhesion molecule 1 (ICAM-1), as does the major group of
HRVs; unlike HRVs, however, it is stable at acid pH. The cryoelectron
microscopy (cryoEM) image reconstruction of CAV21 is consistent with
the highly homologous crystal structure of poliovirus 1; like other
enteroviruses and HRVs, CAV21 has a canyon-like depression around each
of the 12 fivefold vertices. A cryoEM reconstruction of CAV21 complexed
with ICAM-1 shows all five domains of the extracellular component of
ICAM-1. The known atomic structure of the ICAM-1 amino-terminal domains
D1 and D2 has been fitted into the cryoEM density of the complex. The
site of ICAM-1 binding within the canyon of CAV21 overlaps the site of
receptor recognition utilized by rhinoviruses and polioviruses. Interactions within this common region may be essential for triggering viral destabilization after attachment to susceptible cells.
Enteroviruses, parechoviruses, and
human rhinoviruses (HRVs) are closely related viruses belonging to the
family Picornaviridae. Based on genome organization and RNA
sequences, the genera Rhinovirus and Enterovirus
are more closely related to each other than to the rest of the
picornaviruses (15). Whereas HRVs are labile at acid pH,
enteroviruses and parechoviruses are stable over a wider pH range. In
general, the serotypes within each genus have greater sequence
similarity to each other than they have to viruses in other genera.
Coxsackieviruses, polioviruses, some echoviruses, and some other
viruses are all classified as enteroviruses but are differentiated by
their pathogenic properties. Historically, coxsackieviruses have been
subdivided into 23 serotypes belonging to group A and 6 serotypes
belonging to group B (32, 42). These groups are
differentiated primarily by the type of lesions observed on infected
newborn mice. More recently, coxsackieviruses have been further
subdivided and assigned to distinct "clusters" within the
Enterovirus genus based on evolutionary kinship (genotypes). Accordingly, coxsackie A virus serotypes 1, 11, 13, 15, 17, and 18 to
24 and poliovirus serotypes 1 to 3 have been combined into cluster C,
although they cause different diseases (15, 38). All
cluster C coxsackie A viruses produce common cold-like symptoms, clinically indistinguishable from those of HRV infections. Furthermore, coxsackievirus A13 (CAV13), CAV18, and CAV21 have been shown to utilize
as their cellular receptor intercellular adhesion molecule 1 (ICAM-1,
or CD54) (9, 43), the same cell surface molecule as that
used by the major group of HRVs to gain entry into cells (13,
49). HRV infections cause the up-regulation of ICAM-1 and,
hence, the recruitment of leukocytes to sites of inflammation (37). Whether a similar up-regulation occurs for CAV21 is
not known at this time.
Many viruses utilize accessory cell surface molecules for cell
recognition or cell entry (11). For instance, CAV21 can
also bind to decay-accelerating factor (DAF, or CD55), although without causing an infection (44). The ICAM-1 and DAF binding
sites appear to be nonoverlapping although spatially close to each
other (45). The structures of ICAM-1 and DAF are totally
different. The extracellular component of ICAM-1 consists of five
tandem immunoglobulin superfamily (IgSF) domains, whereas DAF is
comprised of four short consensus repeat motifs and a
serine-threonine-rich region that links the protein via a
glycosyl-phosphotidylinositol linker to the plasma membrane.
The CAV21 RNA genome has about 80% amino acid sequence identity to
that of polioviruses, which utilize CD155 as their receptor (4,
19, 53), but only about 50% identity to that of HRVs (24). Although there is a slight preference for codon
usage resembling that of HRVs (24), these sequence
comparisons do not explain the receptor preference for CAV21 and
related cluster C coxsackieviruses. Similarly, the minor group of HRVs
has no obvious phylogenetic separation from the major group of HRVs, yet all minor-group HRVs utilize the low-density lipoprotein receptor to initiate infection (21).
The crystal structures of various HRVs and enteroviruses have been
determined at nearly atomic resolution. These include HRV14 (41) and HRV16 (16, 35), both of which
utilize ICAM-1 as a receptor; HRV1A (26) and HRV2
(51), which do not bind ICAM-1; coxsackievirus B3
(33), which utilizes the coxsackievirus-adenovirus receptor as well as DAF; CAV9 (20), which utilizes an
integrin as a receptor (39); and all three poliovirus
serotypes (22, 29, 54), which utilize the poliovirus
receptor, CD155 (4, 19, 53). However, the
three-dimensional atomic resolution structure of CAV21 has yet to be determined.
ICAM-1 is a cell surface molecule that normally binds to leukocyte
function-associated antigen 1 to provide adhesion between leukocytes
and endothelial cells. Apart from being recruited by viral pathogens,
such as HRVs and some coxsackieviruses, as a receptor, ICAM-1 also
binds to erythrocytes that have been infected by the malarial parasite
Plasmodium falciparum (3, 5, 34). The structure
of the two amino-terminal domains of ICAM-1, designated D1D2, has been
determined to nearly atomic resolution, in both partially
unglycosylated (3) and fully glycosylated (7, 28) forms. The amino-terminal domain D1 was found to have an "intermediate" type of IgSF fold, whereas the second domain, D2, has a constant type 2 IgSF structure (8, 18, 52). Amino acid sequence analyses (48) predict that the other three
domains also have IgSF-type folds.
The structures of glycosylated and unglycosylated, two- and five-domain
ICAM-1, when complexed with HRV16 (28, 36) or HRV14
(28), have been determined to a resolution of about 28 Å by cryoelectron microscopy (cryoEM). By fitting the known
X-ray structures of ICAM-1 and HRVs into the envelope of the cryoEM reconstructions of virus-receptor complexes, it has been possible to
determine the nature of the virus-receptor interactions. Similar results were obtained for the complex formed between poliovirus and
CD155 (4, 19, 53), although the structure of CD155 was
based upon homology modeling. In every case, the receptor is a long,
thin, flexible molecule that binds into the canyon, an
~15-Å-deep surface depression on rhinoviruses and
enteroviruses. These results are consistent with the prediction that
receptor molecules would be sufficiently thin to bind to the more
conserved residues in the canyon, at a site that is less accessible to
neutralizing antibodies (40, 41).
We report here a cryoEM image reconstruction, at a resolution of 26 Å, of CAV21 complexed with its primary receptor, ICAM-1, in
which all five domains of the receptor molecule are visible. Although
domain D1 of ICAM-1 binds to a similar site in the CAV21 canyon
vicinity as in HRVs and overlaps the site of binding of CD155 to
poliovirus, the orientation of the receptor molecule relative to the
virus is different for each type of virus. In contrast, ICAM-1 binds
similarly to different HRV serotypes regardless of whether it is
glycosylated or unglycosylated or is present as two- or five-domain structures.
Sample preparation.
CAV21, strain Kuykendall, was obtained
from the American Type Culture Collection, Manassas, Va. (VR-850). The
virus was propagated in H1-HeLa cells two times, and CAV21-specific,
infectious cDNA was prepared and sequenced (E. Rieder and E. Wimmer,
unpublished data). CAV21 derived from the infectious cDNA was
propagated in 3.6 × 107 HeLa cells/ml, suspended in
Dulbecco minimal Eagle medium (Life Technologies) with 10% bovine
serum. The cells were infected with CAV21 at a multiplicity of
infection of 20. After adsorption at room temperature for 1 h
under mild agitation, the cells were diluted to a concentration of
3 × 106 cells/ml with fresh medium. They were allowed
to grow for 9.5 h, after which time they were harvested and lysed
with 1% Nonidet P-40. They were then briefly homogenized and
centrifuged at 4,000 × g to separate the components.
DNase (0.5 mg/ml) was added to permit digestion of nucleic acids for
1 h, followed by the addition of 0.5 mg of trypsin per ml for 10 min to digest protein. Sucrose gradient and CsCl isopycnic
ultracentrifugations were used to purify the virus. Five-domain, fully
glycosylated ICAM-1 lacking the cytoplasmic and transmembrane domains
was kindly provided by J. M. Greve (14). Plaque
reduction assays, used to determine whether the soluble receptor
blocked H1-HeLa cell infection, showed 100% inhibition at 0.46 mg of
ICAM-1 per ml.
CryoEM.
A 50-µl sample of purified CAV21 (6.2 mg/ml) was
incubated with or without (Table 1) 20 µl of 46.3-mg/ml five-domain ICAM-1 (an excess of about nine receptor
molecules per binding site on the virus) for 35 min on ice. CryoEM
specimens were prepared from 3.5-µl aliquots that were applied to
perforated carbon support electron microscope grids and vitrified in
liquid ethane (2). Micrographs were recorded on Kodak
SO-163 film in a Philips CM200 field emission gun (FEG) microscope at a
nominal magnification of 50,000 and a dose level of 18.5 e
0022-538X/01/$04.00+0 DOI: 10.1128/JVI.75.5.2444-2451.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
Interaction of Coxsackievirus A21 with Its Cellular
Receptor, ICAM-1
ABSTRACT
Top
Abstract
Introduction
Materials and Methods
Results and Discussion
References
INTRODUCTION
Top
Abstract
Introduction
Materials and Methods
Results and Discussion
References
MATERIALS AND METHODS
Top
Abstract
Introduction
Materials and Methods
Results and Discussion
References
/Å2. Micrographs were taken at
different underfocus levels (Table 1) so that useful contrast transfer
function corrections could be achieved uniformly for all resolutions.
The micrographs were digitized on a Zeiss PHODIS microdensitometer at
7-µm intervals but, for computational reasons, the pixels were
averaged to produce 14-µm pixels (2.80-Å spacing at the
specimen). Particles of the virus-receptor complex were boxed from
scanned micrographs with a radius of 130 pixels (364 Å).
TABLE 1.
Electron microscopy data collection and processing
Difference map calculations and model fitting.
CryoEM image
reconstructions were made for native CAV21 and for CAV21 complexed with
five-domain ICAM-1 (Fig. 1). The size of
each map was scaled to that of a map of poliovirus 1 obtained from
X-ray diffraction coordinate data (Protein Data Bank accession number
2PLV) and calculated to approximately the same resolution. The maps
were scaled by comparing the densities within the protein shell (108- to 144-Å radii). A difference map was calculated by
subtracting the virus map from the virus-receptor map.
|
|
Structure of CAV21. The atomic coordinates of poliovirus 1 were used as a basis for building a model of CAV21. Residue replacement and energy minimization were performed with the program SEGMOD (30). The footprint of the ICAM-1 molecule on the CAV21 surface was defined by the residues on the viral surface that have any atoms within 4 Å of any atom in the receptor.
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RESULTS AND DISCUSSION |
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|
Top
Abstract
Introduction
Materials and Methods
Results and Discussion
References
|
|---|
Structure of ICAM-1.
The 180-Å-long structure (Fig.
1 and 3) of the complete extracellular
component of five-domain ICAM-1 bound to CAV21 is clearly visible in
the reconstruction. However, only the first three domains were visible
in an earlier reconstruction of HRV16 complexed with five-domain ICAM-1
(28). The difference may partially reflect the use of
about 200 particle images in the present reconstruction, compared to
only 43 in the earlier reconstruction. In addition, the use of an
electron microscope fitted with an FEG provided better image
conditions because the electron beam was brighter and more
coherent than in conventional instruments. The importance of the
data collected with the FEG was confirmed in that an earlier reconstruction of the CAV21-ICAM-1 complex, obtained with a Philips 420 electron microscope (data not shown), did not show the complete ICAM-1 molecule. Some flexibility of the articulated ICAM-1 molecule is
apparent because the height of the density decreases in successive domains. If the mean height of the density in the viral capsid coat is
arbitrarily set to a value of 10, the densities in domains 1, 2, 3, 4, and 5 are 10, 10, 6, 3, and 1, respectively. Although the density
progressively decreases toward the C terminus of ICAM-1, it is
surprising that the long ICAM-1 molecule is sufficiently rigid for all
domains to remain visible even after the icosahedral averaging inherent
in the reconstruction technique has been applied. It was reported
(47) that ICAM-1 is kinked between domains 2 and 3, but
this orientation does not appear in the present reconstruction. Kirchhausen et al. (27) suggested that ICAM-1 is slightly
kinked between domains 3 and 4, an observation that is approximately consistent with the structure reported here (Fig. 1 and 3). All the
various receptor molecules utilized by picornaviruses are long, thin,
and articulated at hinges between domains. Although ICAM-1 appears to
be more rigid than expected, its properties are consistent with the
requirement that the receptor be a molecule able to flex sufficiently
to recognize additional sites on the viral surface once the first
receptor has been bound. The apparent preference for long, thin, hinged
receptor molecules may be essential for the recruitment of successive
receptors to the viral surface after the initial recognition event.
|
|
Location of the receptor binding site.
The interactions of
ICAM-1 with the surface of CAV21 span between the "north" and
"south" canyon rims (Fig. 4), involving 
C and the loop from E
to 
B of viral protein 1 (VP1) on the north rim, the GH loops of VP1
and VP3 on the floor, and the "puff" on the south rim. The puff is
a variably sized insertion in VP2 of picornaviruses (41).
|
|
barrel containing an as-yet-unidentified "pocket factor" (Fig.
4 and 5) (12, 40). It has been suggested that the pocket
factor stabilizes the virus during transit between hosts but is
displaced by the competition of the receptor for its overlapping
binding site (17, 35, 40). Thus, binding of receptor would
destabilize the virion and initiate uncoating. This hypothesis is
consistent with the observed degradation of HRVs in the presence of
soluble ICAM-1 (23) and the possible absence of the pocket
factor in the poliovirus-CD155 complex (4).
Virus stability. The difficulty of determining incubation times and temperatures needed to obtain successful virus-receptor cryoEM images is related to the destabilizing effect of the receptor on the virus. Thus, it is significant that kinetic analyses have shown, both for HRVs (6) and for polioviruses (31), that there are two distinct modes of binding whose relative abundance varies with temperature. The binding modes observed in the cryoEM reconstructions are likely to be the most stable intermediates, although these may be different depending upon the virus-receptor complex. Kolatkar et al. (28) argue that the complexes seen for HRVs are an initial event, consistent with kinetic data (6). In view of the probable loss of the pocket factor from the poliovirus-receptor complex (4) and the more extensive contact of the receptor with the viral surface, it is possible that the poliovirus-receptor complex represents an intermediate stage of picornavirus-receptor interaction. Thus, the CAV21, HRV, and poliovirus interactions with their receptors might represent sequential steps in similar processes for each virus.
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ACKNOWLEDGMENTS |
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We thank Sharon Wilder and Cheryl Towell for help in the preparation of the manuscript.
This work was supported by National Institutes of Health grants to M.G.R. (AI11219) and E.W. (AI32100, AI39485, and AI15122); a National Institutes of Health program project grant to M.G.R., R.J.K., T.S.B., and others (AI45976); and a National Science Foundation shared instrument grant to T.S.B., M.G.R., and others (BIR-9112921). Support was also provided by a Purdue University reinvestment grant.
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FOOTNOTES |
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* Corresponding author. Mailing address: Department of Biological Sciences, Purdue University, West Lafayette, IN 47907-1392. Phone: (765) 494-1164. Fax: (765) 496-1189. E-mail: rjkuhn{at}bragg.bio.purdue.edu.
Present address: School of Biological Sciences, University of
Manchester, Manchester M13 9PT, England.
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References
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around domains D1 and D2, 1.30 
