X-ray structure of a minor group human rhinovirus bound to a fragment of its cellular receptor protein

Versatility in ligand recognition by LDL receptor family proteins: advances and frontiers

“…Other structures containing inter-and intramolecular binding interfaces between LA repeats and their partners also share the essential elements of the recognition mode seen in the LA3-4/RAP-D3 complex ( Figure 3). These complexes include the long-range intramolecular interface between LA repeats four and five and the YWTD beta-propeller domain [14], and a VLDLR fragment bound to human rhinovirus serotype 2 (HRV2), for which the LDLR and VLDLR serve as the primary receptor for cell entry [15]. In the structure of the giant erythrocruorin respiratory complex from the earthworm Lumbricus terrestris, interactions between the LA repeats of three linker chains with the hemoglobin b subunits of the complex also exhibit this canonical binding mode with a minor variation: the basic side chains projecting into the acidic pocket are from arginine residues, rather than from lysines [16].…”

“…This binding mode also appears to be tailored for a multivalent kind of recognition, because of the small area contributed by each LA repeat to the interface. Thus, two repeats are used in the LA3-4/RAP-D3 interface, multirepeat fragments exhibit much higher affinity for the HRV2 capsid than single repeats [15], and the LA4-5 pair of repeats is needed to establish the longrange interface with the propeller domain at endosomal pH [14].…”

The Minor Receptor Group of Human Rhinovirus (HRV) Includes HRV23 and HRV25, but the Presence of a Lysine in the VP1 HI Loop Is Not Sufficient for Receptor Binding

“…Comparison of the VP1 sequences of all HRVs within the regions equivalent to the site of binding of module 3 of VLDLR to HRV2 (36) revealed the presence of a lysine in the HI loop in the serotypes listed in Fig. 1.…”

“…Subsequently, 24 (1) and finally 100 serotypes (counting the subtypes HRV1A and HRV1B as one strain) were assigned to the two receptor groups by using cross-competition and inhibition of cell binding by a monoclonal antibody recognizing intercellular adhesion molecule 1 (ICAM-1), the receptor of the major group of HRVs (32,33,35). According to these reports, 90 serotypes bind ICAM-1, whereas both subtypes of HRV1 (HRV1A and HRV1B) and 8 other serotypes were categorized as belonging to the minor group; they were later shown to use members of the low-density-lipoprotein receptor (LDLR) family for cell entry (12,20,36). HRV87 was noted to be an exception in that it binds a sialylated membrane protein.…”

“…We have previously shown that a soluble recombinant fusion protein composed of the maltose binding protein (MBP) and an artificial concatemer of five copies of repeat 3 (V3) of VLDLR arranged in tandem (MBP-V33333) exhibits strong virus neutralization capacity toward the 10 minor group HRVs (36). Therefore, by using cell protection assays with this protein, ligand blots, and replication in COS-7 cells that do not express ICAM-1, we investigated the nature of the strains containing a lysine residue in the HI loop and found that HRV23 and HRV25 possess all characteristics of minor group viruses.…”