Membrane Recognition by Vesicular Stomatitis Virus Involves Enthalpy-Driven Protein-Lipid Interactions

Carneiro, Fabiana A.; Bianconi, M. Lucia; Weissmüller, Gilberto; Stauffer, Fausto; Poian, Andrea T. Da

doi:10.1128/jvi.76.8.3756-3764.2002

Cited by 91 publications

(88 citation statements)

References 58 publications

(63 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Membrane fusion mediated by VSV G protein reconstituted in lipid vesicles showed a large preference for target membranes containing PS or phosphatidic acid (42). We found that the extent of pHinduced conformational changes of G protein depends on the number of negative charges in the target membrane and that G protein-mediated membrane fusion may be correlated with the PS content in the vesicles (35). Although our results unequivocally demonstrate the importance of electrostatic interactions for VSV fusion, we cannot exclude the possibility that hydrophobic interactions are also involved in VSV interaction with membranes during fusion.…”

Section: Role Of Phosphatidylserinecontrasting

confidence: 42%

“…This indicates that the protonation of a small number of ionizable groups is required for G protein structural changes, suggesting that the protonation of the imidazole ring of histidyl residue(s) (pK = 6.0) is involved in G protein conformational changes required for fusion. In addition, we have found that VSV binding to membranes as well as the fusion reaction itself were highly dependent on electrostatic interactions between negative charges on the membrane surface and positively charged amino acids in G protein at the fusion pH (35), and His becomes positively charged after protonation ( Figure 3). For rabies virus, Roche and Gaudin (43), showed that the pK of the transition from the native to the fusion-inactive state of G protein is 6.65, also suggesting that His residues are involved.…”

Section: Role Of Histidinesmentioning

confidence: 99%

Section: Rhabdovirus Binding To the Cell Surfacementioning

confidence: 99%

“…Isothermal titration calorimetry experiments have shown that VSV binding to liposomes is an enthalpically driven process, suggesting that electrostatic interactions are important for membrane recognition (35). Using atomic force microscopy we determined the forces of VSV G protein binding to lipid films of different composition (35,36). We measured forces as strong as 2 nN after virus interaction with a PScontaining lipid film, whereas no interaction between the virus and membranes composed of neutral phospholipids was observed (35).…”

Section: Rhabdovirus Binding To the Cell Surfacementioning

confidence: 99%

“…Using atomic force microscopy we determined the forces of VSV G protein binding to lipid films of different composition (35,36). We measured forces as strong as 2 nN after virus interaction with a PScontaining lipid film, whereas no interaction between the virus and membranes composed of neutral phospholipids was observed (35).…”

Section: Rhabdovirus Binding To the Cell Surfacementioning

confidence: 99%

See 4 more Smart Citations

Viral membrane fusion: is glycoprotein G of rhabdoviruses a representative of a new class of viral fusion proteins?

Poian

Carneiro

Stauffer

2005

Braz J Med Biol Res

View full text Add to dashboard Cite

Enveloped viruses always gain entry into the cytoplasm by fusion of their lipid envelope with a cell membrane. Some enveloped viruses fuse directly with the host cell plasma membrane after virus binding to the cell receptor. Other enveloped viruses enter the cells by the endocytic pathway, and fusion depends on the acidification of the endosomal compartment. In both cases, virus-induced membrane fusion is triggered by conformational changes in viral envelope glycoproteins. Two different classes of viral fusion proteins have been described on the basis of their molecular architecture. Several structural data permitted the elucidation of the mechanisms of membrane fusion mediated by class I and class II fusion proteins. In this article, we review a number of results obtained by our laboratory and by others that suggest that the mechanisms involved in rhabdovirus fusion are different from those used by the two well-studied classes of viral glycoproteins. We focus our discussion on the electrostatic nature of virus binding and interaction with membranes, especially through phosphatidylserine, and on the reversibility of the conformational changes of the rhabdovirus glycoprotein involved in fusion. Taken together, these data suggest the existence of a third class of fusion proteins and support the idea that new insights should emerge from studies of membrane fusion mediated by the G protein of rhabdoviruses. In particular, the elucidation of the three-dimensional structure of the G protein or even of the fusion peptide at different pH's might provide valuable information for understanding the fusion mechanism of this new class of fusion proteins. Correspondence

show abstract

Section: Role Of Phosphatidylserinecontrasting

confidence: 42%

Section: Role Of Histidinesmentioning

confidence: 99%

Section: Rhabdovirus Binding To the Cell Surfacementioning

confidence: 99%

Section: Rhabdovirus Binding To the Cell Surfacementioning

confidence: 99%

Section: Rhabdovirus Binding To the Cell Surfacementioning

confidence: 99%

See 3 more Smart Citations

Viral membrane fusion: is glycoprotein G of rhabdoviruses a representative of a new class of viral fusion proteins?

Poian

Carneiro

Stauffer

2005

Braz J Med Biol Res

View full text Add to dashboard Cite

show abstract

Functionalized Graphene as Extracellular Matrix Mimics: Toward Well‐Defined 2D Nanomaterials for Multivalent Virus Interactions

Gholami

Lauster

Ludwig

et al. 2017

Adv Funct Materials

View full text Add to dashboard Cite

Polysulfated nanomaterials that mimic the extracellular cell matrix are of great interest for their potential to modulate cellular responses and to bind and neutralize pathogens. However, control over the density of active functional groups on such biomimetics is essential for efficient interactions, and this remains a challenge. In this regard, producing polysulfated graphene derivatives with control over their functionality is an intriguing accomplishment in order to obtain highly effective 2D platforms for pathogen interactions. Here, a facile and efficient method for the controlled attachment of a heparin sulfate mimic on the surface of graphene is reported. Dichlorotriazine groups are conjugated to the surface of graphene by a one-pot [2+1] nitrene cycloaddition reaction at ambient conditions, providing derivatives with defined functionality. Consecutive step by step conjugation of hyperbranched polyglycerol to the dichlorotriazine groups and eventual conversion to the polyglycerol sulfate result in the graphene based heparin biomimetics. Scanning force microscopy, cryo-transmission electron microscopy, and in vitro bioassays reveal strong interactions between the functionalized graphene (thoroughly covered by a sulfated polymer) and vesicular stomatitis virus. Infection experiments with highly sulfated versions of graphene drastically promote the infection process, leading to higher viral titers compared to nonsulfated analogues.

show abstract

Differential distribution of L-aspartate- and L-glutamate-immunoreactive structures in the arcopallium and medial striatum of the domestic chick (Gallus domesticus)

Ádám

Csillag

2006

J. Comp. Neurol.

View full text Add to dashboard Cite

The role of amino acid neurotransmitters in learning and memory is well established. We investigated the putative role of L-aspartate as a neurotransmitter in the arcopallial-medial striatal pathway, which is known to be involved in passive avoidance learning in domestic chicks. Double immunocytochemistry against L-aspartate and L-glutamate was performed at both light and electron microscopic levels. L-aspartate- and L-glutamate-immunoreactive neurons in the arcopallium and posterior amygdaloid pallium were identified and counted by using fluorescence microscopy and confocal laser scanning microscopy. Most labeled neurons of arcopallium were enriched in glutamate as well as aspartate. However, the arcopallium and posterior amygdaloid pallium differed from a neighboring telencephalic region (nidopallium; formerly neostriatum) by containing a substantial proportion of cells singly labeled for L-aspartate (15%, vs. 5.3% in the nidopallium). Aspartate-labeled neurons constitute approximately 20%, 25%, 42%, and 28% of total in the posterior amygdaloid pallium and the medial, dorsal, and anterior arcopallia, respectively. Immunoelectron microscopy showed that L-aspartate was enriched in terminals of the medial striatum. The labeled terminals had clear and round vesicles and asymmetric junctions; similar to those immunoreactive to L-glutamate. Axon terminals singly labeled for L-aspartate made up 17% of the total. In addition, 7% of neuronal perikarya and 26% of all dendritic profiles appeared to be labeled specifically with L-aspartate but not L-glutamate. The results indicate that L-aspartate may play a specific role (as distinct from that of L-glutamate) in the intrinsic and extrinsic circuits instrumental in avian learning and memory.

show abstract

Membrane Recognition by Vesicular Stomatitis Virus Involves Enthalpy-Driven Protein-Lipid Interactions

Cited by 91 publications

References 58 publications

Viral membrane fusion: is glycoprotein G of rhabdoviruses a representative of a new class of viral fusion proteins?

Viral membrane fusion: is glycoprotein G of rhabdoviruses a representative of a new class of viral fusion proteins?

Functionalized Graphene as Extracellular Matrix Mimics: Toward Well‐Defined 2D Nanomaterials for Multivalent Virus Interactions

Differential distribution of L-aspartate- and L-glutamate-immunoreactive structures in the arcopallium and medial striatum of the domestic chick (Gallus domesticus)

Contact Info

Product

Resources

About