Functional implications of the structure of the murine parvovirus, minute virus of mice

Agbandje‐McKenna, Mavis; Llamas-Saíz, Antonio L.; Wang, Feng; Tattersall, Peter; Rossmann, Michael G.

doi:10.1016/s0969-2126(98)00137-3

Cited by 191 publications

(275 citation statements)

References 55 publications

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“…An O 2 workstation (Silicon Graphics, Mountain View, CA), the PDB coordinates of MVM strain i (MVMi) (1MVM) (35,36), and the programs INSIGHTII (Biosym Technologies, San Diego), RASMOL (49), and WHATIF (50) were used.…”

Section: Molecular Graphics and Structuralmentioning

confidence: 99%

“…We have inspected the noncovalent contacts between trimeric subassemblies in the crystallographic structure of the MVMi virion (35,36). Within the imposed limits (cutoff distance 0.5 Å higher than the sum of the van der Waals radii of the two atoms considered), a total of 104 residues of the 587 amino acids per capsid monomer (VP2) were found to be involved in intertrimeric atomic contacts in MVM.…”

Section: Analysis Of Intertrimeric Interactions and Selection Of Intementioning

confidence: 99%

“…1). In the minute virus of mice (MVM) (35,36), as in other parvoviruses, VP2 (the major capsid protein) is able to self-assemble into empty capsids, known as virus-like particles (VLPs) (38). VP1 includes the VP2 sequence plus a N-terminal extension (39).…”

mentioning

confidence: 99%

“…VP3 results from the cleavage of the N terminus of some VP2 subunits (40). Intersubunit contacts in the parvovirus capsid essentially involve residues and structural elements that are shared by all three proteins, and both the structure and physical properties, including thermostability, of parvovirus VLPs are very similar to those of natural capsids (32,33,36,38,41,42).…”

mentioning

confidence: 99%

“…The icosahedral T ϭ 1 capsids of parvoviruses (32)(33)(34)(35)(36)(37) are formed by 60 protein subunits that are contributed by three nonidentical polypeptide chains (VP1, VP2, and VP3). These polypeptides derive, however, from a single gene and show identical fold and core sequence (Fig.…”

mentioning

confidence: 99%

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Role of interfacial amino acid residues in assembly, stability, and conformation of a spherical virus capsid

Reguera

Carreira

Riolobos

et al. 2004

Proc. Natl. Acad. Sci. U.S.A.

126

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Twenty-eight amino acid residues involved in most noncovalent interactions between trimeric protein subunits in the capsid of the parvovirus minute virus of mice were truncated individually to alanine, and the effects on capsid assembly, thermostability, and conformation were analyzed. Only seven side chains were essential for protein subunit recognition. These side chains virtually corresponded with those that either buried a large hydrophobic surface on trimer association or formed buried intertrimer hydrogen bonds or salt bridges. The seven residues are evolutionarily conserved, and they define regularly spaced spots on a thin equatorial belt surrounding each trimer. Truncation of the many side chains that were dispensable for assembly, including those participating in solvent-accessible polar interactions, did not substantially affect capsid thermostability either. However, the interfacial residues located at the base of the pores delineating the capsid five-fold axes participated in a heat-induced conformational rearrangement associated with externalization of the capsid protein N terminus, and they were needed for infectivity. Thus, at the subunit interfaces of this model virus capsid, only key residues involved in the strongest interactions are critical for assembly and stability, but additional residues fulfill other important biological roles. P rotein-protein recognition mediates many fundamental biological processes. A detailed knowledge of these processes requires the determination of the structural, energetic, and functional roles of individual amino acid residues and interactions in protein-protein interfaces. These studies have been generally undertaken by using small protein-ligand complexes or oligomeric proteins of moderate size (reviewed in ref. 1; see also refs. 2-4). In contrast, for multimeric protein complexes, such as viral capsids (5, 6) or large cellular assemblies, little is known about the specific molecular determinants of protein association and stability. Mutational studies of virus capsids, generally focused on a few specific amino acid residues, have provided important insights (7-22). However, exhaustive experimental studies on the relative importance of residues and molecular interactions in viral capsid assembly, disassembly, and͞or stability are still very limited. These studies contribute also to the understanding of protein structure-function relationships and evolution under conflictive selective constraints (22-27), and they could be exploited possibly in the design of thermostable vaccines and antiviral agents promoting capsid disassembly or interfering with assembly (23, 28-31).Many viruses, including viruses of medical or veterinary significance, have capsids of icosahedral symmetry. The icosahedral T ϭ 1 capsids of parvoviruses (32-37) are formed by 60 protein subunits that are contributed by three nonidentical polypeptide chains (VP1, VP2, and VP3). These polypeptides derive, however, from a single gene and show identical fold and core sequence (Fig. 1). In the minut...

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Section: Molecular Graphics and Structuralmentioning

confidence: 99%

Section: Analysis Of Intertrimeric Interactions and Selection Of Intementioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

See 3 more Smart Citations

Role of interfacial amino acid residues in assembly, stability, and conformation of a spherical virus capsid

Reguera

Carreira

Riolobos

et al. 2004

Proc. Natl. Acad. Sci. U.S.A.

126

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Parvoviruses

Tattersall¹,

Cotmore²

2010

Topley &Amp; Wilson's Microbiology and Microbial Infections

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Protein Nanoparticles: Uniting the Power of Proteins with Engineering Design Approaches

Habibi

Mauser

et al. 2022

Advanced Science

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Protein nanoparticles, PNPs, have played a long‐standing role in food and industrial applications. More recently, their potential in nanomedicine has been more widely pursued. This review summarizes recent trends related to the preparation, application, and chemical construction of nanoparticles that use proteins as major building blocks. A particular focus has been given to emerging trends related to applications in nanomedicine, an area of research where PNPs are poised for major breakthroughs as drug delivery carriers, particle‐based therapeutics or for non‐viral gene therapy.

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Functional implications of the structure of the murine parvovirus, minute virus of mice

Cited by 191 publications

References 55 publications

Role of interfacial amino acid residues in assembly, stability, and conformation of a spherical virus capsid

Role of interfacial amino acid residues in assembly, stability, and conformation of a spherical virus capsid

Parvoviruses

Protein Nanoparticles: Uniting the Power of Proteins with Engineering Design Approaches

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