Structural studies on the Ebola virus matrix protein VP40 indicate that matrix proteins of enveloped RNA viruses are analogues but not homologues

Timmins, Joanna; Ruigrok, Rob W.H.; Weissenhorn, Winfríed

doi:10.1016/j.femsle.2004.03.002

Cited by 23 publications

(34 citation statements)

References 68 publications

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“…Despite functional and structural homology with VP40, membrane binding modes appear to differ significantly between the 2 viruses. VP40 has been observed in multiple oligomeric forms; oligomerization occurs via the N-terminal domain to form monomeric, dimeric, hexameric, and octameric species (10,17,18,(30)(31)(32). In contrast, BDV-M has been observed in only 2 oligomeric states (15,16), namely tetramers and octamers.…”

Section: Discussionmentioning

confidence: 99%

“…These M-proteins exhibit neither sequence nor structural homology to one other (10). Here, we report the 3D structure of BDV-M, a full-length M-protein structure of a nonsegmented NSV, and show that the peripheral membrane protein binds ssRNA oligonucleotides.…”

mentioning

confidence: 83%

“…M-proteins of several negative-strand RNA viruses (NSVs) are also involved in the regulation of virus replication and transcription and in the transport of ribonucleoprotein (RNP) complexes (9)(10)(11)(12)(13). BDV-M, the M-protein of BDV, is the smallest M-protein (16.2 kDa) among all NSVs.…”

mentioning

confidence: 99%

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Crystal structure of the Borna disease virus matrix protein (BDV-M) reveals ssRNA binding properties

Neumann¹,

Lieber²,

Meyer³

et al. 2009

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

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 83%

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Crystal structure of the Borna disease virus matrix protein (BDV-M) reveals ssRNA binding properties

Neumann¹,

Lieber²,

Meyer³

et al. 2009

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

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“…A number of matrix-like proteins are known to bind membranes or lipid vesicles in vitro, most likely through a combination of hydrophobic and electrostatic interactions (12)(13)(14). Expression of certain Ms in eukaryotic cells in the absence of other viral proteins can induce formation of virus-like particles (VLPs).…”

mentioning

confidence: 99%

Surface features of a Mononegavirales matrix protein indicate sites of membrane interaction

Money

McPhee²,

Mosely³

et al. 2009

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

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The matrix protein (M) of respiratory syncytial virus (RSV), the prototype viral member of the Pneumovirinae (family Paramyxoviridae, order Mononegavirales), has been crystallized and the structure determined to a resolution of 1.6 Å. The structure comprises 2 compact ␤-rich domains connected by a relatively unstructured linker region. Due to the high degree of side-chain order in the structure, an extensive contiguous area of positive surface charge covering Ϸ600 Å 2 can be resolved. This unusually large patch of positive surface potential spans both domains and the linker, and provides a mechanism for driving the interaction of the protein with a negatively-charged membrane surface or other virion components such as the nucleocapsid. This patch is complemented by regions of high hydrophobicity and a striking planar arrangement of tyrosine residues encircling the C-terminal domain. Comparison of the RSV M sequence with other members of the Pneumovirinae shows that regions of divergence correspond to surface exposed loops in the M structure, with the majority of viral species-specific differences occurring in the N-terminal domain.CD ͉ crystal structure ͉ respiratory syncytial virus ͉ sequence alignment R espiratory syncytial virus (RSV) is the prototype member of the Pneumovirinae, a subfamily of the Paramyxoviridae (order Mononegavirales). Morphologically, the extracellular virion consists of a lipid bilayer envelope, within which are embedded 3 glycoproteins, 2 of which (F and G) are important in cell attachment and viral entry into target cells. The third, the SH protein, contributes to pathology in the host (1). Internally, virions contain helical nucleocapsids that consist of N protein tightly bound to the negative-sense nonsegmented genomic RNA. The nucleocapsid in turn is associated with components of the viral RNA-dependent RNA polymerase (L, P, M2-1, and M2-2 proteins), forming the holo-nucleocapsid (2-4). Between the holo-nucleocapsid and the outer envelope there is a layer of matrix protein (M), which is associated peripherally with the membrane (5). The other family members of the Mononegavirales (Rhabdoviridae, Filoviridae, and Bornaviridae) all subscribe to this basic arrangement of the virion, although the overall morphology can vary between the families. For example, Paramyxoviridae virions are pleiomorphic, whereas the Rhabdoviridae have a regular bullet shape structure, and the Filoviridae have a more filamentous shape. Extracellular RSV virions form by a budding process that occurs at the plasma membrane within specialized lipid domains (5, 6) and M appears to drive the final assembly process, which is the incorporation of the holo-nucleocapsid and initiation of the budding process (7,8). Before budding, there is a coordinated assembly of viral components; and it is evident that the glycoproteins and M proteins are important determinants of the location on the plasma membrane at which the virus buds (9). It is also possible that the interaction between M and the glycoproteins, possibly mediat...

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“…Though similar in function, the sequence homology of the M proteins from filo-, rhabdo-, myxo-, and paramyxovirus and retroviral MA do not show clear homology although the L domains of PS/TAP or PY motifs are similar in these proteins that function in budding of virions from host cells (40,79,80,119,216). Comparison of the structural homology has been examined by structural biologists in reviews of the literature between Ebola virus VP40, VSV M, and HIV MA and these were found to have no structural homology (200), but a comparison between influenza virus M1 and HIV MA and CA proteins revealed that the M1 protein may have a combination of the important structural assembly elements of the MA and CA proteins (77). Taken together these observations show that trying to find the evolutionary link between proteins from RNA viruses is a complicated endeavor.…”

Section: Enveloped Rna Viruses: Origins and M Proteinsmentioning

confidence: 99%

Investigation of the Vesicular Stomatitis Virus Matrix Protein: Uncoating and Assembly

Mire¹

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Structural studies on the Ebola virus matrix protein VP40 indicate that matrix proteins of enveloped RNA viruses are analogues but not homologues

Cited by 23 publications

References 68 publications

Crystal structure of the Borna disease virus matrix protein (BDV-M) reveals ssRNA binding properties

Crystal structure of the Borna disease virus matrix protein (BDV-M) reveals ssRNA binding properties

Surface features of a Mononegavirales matrix protein indicate sites of membrane interaction

Investigation of the Vesicular Stomatitis Virus Matrix Protein: Uncoating and Assembly

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