Fusion and Haemolysis of Erythrocytes caused by Three Togaviruses: Semliki Forest, Sindbis and Rubella

Väänänen, Pertti; Kääriäinen, Leevi

doi:10.1099/0022-1317-46-2-467

Cited by 77 publications

(24 citation statements)

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“…This is closely related to the observation of hemolysis and fusion in acid (pH '6.0) by togaviruses such as Semliki forest, Sindbis, and rubella (2,3). Fusion of Semliki forest virus with lipid liposomes in acid has also been observed (4,5).…”

supporting

confidence: 54%

Interaction of influenza virus hemagglutinin with target membrane lipids is a key step in virus-induced hemolysis and fusion at pH 5.2.

Maeda¹,

Kawasaki²,

Ohnishi³

1981

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

163

114

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Interaction of influenza virus hemagglutinin with target membrane lipids is a key step in virus-induced hemolysis and fusion at McConnell, March 30, 1981 ABSTRACT The molecular mechanism of hemolysis and fusion by influenza virus in acidic media was studied. First, the effect of trypsin treatment on the activity of fibroblast-grown influenza virus was studied. The results showed that the split form of viral hemagglutinin, HA1 and HA2, but not the precursor, is responsible for the activity. Second, the interaction of egg-grown influenza virus, which contains the split hemagglutinin, with lipid liposomes was studied by spin labeling and electron microscopy. Phospholipid transfer from the viral envelope to the lipid bilayer membrane occurred within 30 s at pH 4.5-5.4. The transfer is largely independent ofthe lipid composition and the crystalline vs. liquid/ crystalline state ofthe membrane. Virus-induced lysis ofliposomes also took place rapidly in the same pH range. Envelope fusion with liposomes occurred at pH 5.2 but not at pH 7.0. These characteristic interactions were similar to those between influenza virus and erythrocytes reported previously. On the other hand, hemagglutinating virus ofJapan did not interact with liposomes at neutral pH. These results suggest that protonation of the NH2-terminal segment of the HA2 form causes interaction of the segment with the lipid core ofthe target cell membrane, leading to hemolysis and fusion.

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supporting

confidence: 54%

Interaction of influenza virus hemagglutinin with target membrane lipids is a key step in virus-induced hemolysis and fusion at pH 5.2.

Maeda¹,

Kawasaki²,

Ohnishi³

1981

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

163

114

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“…It should be noted, however, that virus exposed to acid or neutral pH did cause some hemolysis; A readings from control erythrocyte samples without virus were subtracted from the values obtained with virus. Thus, unlike Semliki Forest virus and influenza virus, which hemolyze well only at acidic pH (18)(19)(20), Sendai virus is active over a pH range from 5 to 9, and shows no significant difference in hemolysis between pH 5 and 7. The hemagglutinating titer per unit of viral protein was determined for each virus preparation after exposure to different pHs, and no difference in hemagglutinating activity was found (data not shown).…”

Section: Resultsmentioning

confidence: 95%

Enhancement of membrane-fusing activity of sendai virus by exposure of the virus to basic pH is correlated with a conformational change in the fusion protein.

Hsu¹,

Scheid²,

Choppin³

1982

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

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Enhancement of membrane-fusing activity of Sendai virus by exposure of the virus to basic pH is correlated with a conformational change in the fusion protein Contributed by Purmell W. Choppin, July 6, 1982 ABSTRACT The effect of pH on the membrane-fusion activity of Sendai virus was examined (pH 5.0-9.5) by using, as assays of activity, hemolysis of chicken erythrocytes and the fusion of baby hamster kidney (BHK-21) cells. Exposure of virus to basic pH increased fusion activity; the optimum pH was found to be 9.0. All assays were carried out at pH 7.0, and the virus retained enhanced fusion activity after it was exposed to basic pH and returned to neutral pH. The enhanced fusion activity was correlated with an irreversible conformational change in the fusion protein (F protein) of the virus, as demonstrated by a change in the circular dichroism spectrum of the protein.

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“…The ability of Sindbis virus glycoprotein to induce cell-cell fusion after brief exposure to acid pH has been well characterized (30,49). In BHK cells, it has been shown that this process is a two-step event requiring exposure to pH 5.3 followed by a return to pH 7.2 for optimal fusion to be observed (15,30,37).…”

mentioning

confidence: 99%

Single Amino Acid Insertions at the Junction of the Sindbis Virus E2 Transmembrane Domain and Endodomain Disrupt Virus Envelopment and Alter Infectivity

Hernandez

Ferreira

Sinodis

et al. 2005

J Virol

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The final steps in the envelopment of Sindbis virus involve specific interactions of the E2 endodomain with the virus nucleocapsid. Deleting E2 K at position 391 (E2 ⌬K391) resulted in the disruption of virus assembly in mammalian cells but not insect cells (host range mutant). This suggested unique interactions of the E2 ⌬K391 endodomain with the different biochemical environments of the mammalian and insect cell lipid bilayers. To further investigate the role of the amino acid residues located at or around position E2 391 and constraints on the length of the endodomain on virus assembly, amino acid insertions/substitutions at the transmembrane/endodomain junction were constructed. An additional K was inserted at amino acid position 392 (KK391/392), a K3F substitution at position 391 was constructed (F391), and an additional F was inserted at 392 (FF391/392). These changes should lengthen the endodomain in the KK391/392 insertion mutant or shorten the endodomain in the FF391/392 mutant. The mutant FF391/392 grown in BHK cells formed virus particles containing extruded material not found on wild-type virus. This characteristic was not seen in FF391/392 virus grown in insect cells. The mutant KK391/392 grown in BHK cells was defective in the final membrane fission reaction, producing multicored or conjoined virus particles. The production of these aberrant particles was ameliorated when the KK391/392 mutant was grown in insect cells. These data indicate that there is a critical minimal spanning distance from the E2 membrane proximal amino acid at position 391 and the conserved E2 Y400 residue. The observed phenotypes of these mutants also invoke an important role of the specific host membrane lipid composition on virus architecture and infectivity.The alphavirus Sindbis is an excellent model for the study of the assembly of membrane-containing viruses. Unlike the majority of enveloped viruses, which are loosely structured protein modified membrane envelopes, the alphaviruses are highly organized icosahedral protein shells with an associated membrane (17,36,40). The three proteins of Sindbis virus are organized into two nested protein shells with T ϭ 4 icosahedral symmetry (38). The outer protein shell contains 240 copies of glycoproteins E1 and E2. The inner protein shell contains 240 copies of the capsid protein C which are assembled around the plus-sense single-stranded RNA (48). The structure of the virus is stabilized through specific E1-E1 interactions, and anchoring of the outer protein shell to the inner protein shell occurs through specific associations of the E2 glycoproteins with the capsid proteins across the intervening host cell membrane (1, 22, 23). The E2-capsid interactions are acquired in the final stages of virus assembly as the virus capsid is enveloped in the E1-E2 modified plasma membrane (5, 27). These E2-capsid interactions occur for each of the 240 copies of E2 and capsid protein holding the mature virion in a high energy, metastable conformation (2,8,34). Energy stored in the E1 glycoprot...

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Fusion and Haemolysis of Erythrocytes caused by Three Togaviruses: Semliki Forest, Sindbis and Rubella

Cited by 77 publications

References 1 publication

Interaction of influenza virus hemagglutinin with target membrane lipids is a key step in virus-induced hemolysis and fusion at pH 5.2.

Interaction of influenza virus hemagglutinin with target membrane lipids is a key step in virus-induced hemolysis and fusion at pH 5.2.

Enhancement of membrane-fusing activity of sendai virus by exposure of the virus to basic pH is correlated with a conformational change in the fusion protein.

Single Amino Acid Insertions at the Junction of the Sindbis Virus E2 Transmembrane Domain and Endodomain Disrupt Virus Envelopment and Alter Infectivity

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