Encephalitogenicity of measles virus in marmosets

Albrecht, Paul; Lorenz, Douglas E.; Klutch, M J

doi:10.1128/iai.34.2.581-587.1981

Cited by 20 publications

(15 citation statements)

References 9 publications

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“…However, the animals did seroconvert, which may indicate the existence of a subclinical or local infections caused by limited uptake of the virus. These results seem to confirm previous findings (2) showing that marmosets infected intracerebrally with Edmonston virus developed encephalitis but displayed no visceral symptoms; vaccination by the intranasal and intradermal routes protected the animal, indicating seroconversion. The small amounts of undeleted forms of CD46 which we found in the marmoset brain are consistent with the ability of Edmonston measles virus to cause encephalitis.…”

Section: Most Organs Of the Common Marmoset Contain Cd46 Molecules Wisupporting

confidence: 91%

“…Wild-type virus could be detected in peripheral blood cells of infected marmosets by RT-PCR, but tests for the Edmonston strain in the other group of marmosets were negative. In our experiments, the marmosets, although clearly infected with wild-type virus, did not exhibit the severe symptoms observed by Albrecht et al (1,2), and none of the animals died. This difference may be related to the strain of wild-type measles virus used for inoculation, the species of marmoset, or the improved nutritional state of the animals, which had been reared in captivity.…”

Section: Most Organs Of the Common Marmoset Contain Cd46 Molecules Wisupporting

confidence: 49%

“…Indeed, this appears to be the case, since marmosets inoculated with Edmonston virus developed no symptoms (2). However, other researchers have reported that the common marmoset, moustached tamarin, and squirrel monkeys are susceptible to infections by wild-type virus which causes symptoms including severe gastroenterocolitis, immunosuppression, respiratory congestion, and in some instances rash and Koplik's spots (1,2,27). This basic observation, coupled with the reports that wild-type strains of measles virus were unable to hemagglutinate African green monkey erythrocytes, led us to suspect that natural isolates of the virus used a receptor other than CD46 to bind to the host cell.…”

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confidence: 99%

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A Single Amino Acid Change in the Hemagglutinin Protein of Measles Virus Determines Its Ability To Bind CD46 and Reveals Another Receptor on Marmoset B Cells

Hsu

Sarangi

Iorio

et al. 1998

J Virol

144

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This paper provides evidence for a measles virus receptor other than CD46 on transformed marmoset and human B cells. We first showed that most tissues of marmosets are missing the SCR1 domain of CD46, which is essential for the binding of Edmonston measles virus, a laboratory strain that has been propagated in Vero monkey kidney cells. In spite of this deletion, the common marmoset was shown to be susceptible to infections by wild-type isolates of measles virus, although they did not support Edmonston measles virus production. As one would expect from these results, measles virus could not be propagated in owl monkey or marmoset kidney cell lines, but surprisingly, both a wild-type isolate (Montefiore 89) and the Edmonston laboratory strain of measles virus grew efficiently in B95-8 marmoset B cells. In addition, antibodies directed against CD46 had no effect on wild-type infections of marmoset B cells and only partially inhibited the replication of the Edmonston laboratory strain in the same cells. A direct binding assay with insect cells expressing the hemagglutinin (H) proteins of either the Edmonston or Montefiore 89 measles virus strains was used to probe the receptors on these B cells. Insect cells expressing Edmonston H but not the wild-type H bound to rodent cells with CD46 on their surface. On the other hand, both the Montefiore 89 H and Edmonston H proteins adhered to marmoset and human B cells. Most wild-type H proteins have asparagine residues at position 481 and can be converted to a CD46-binding phenotype by replacement of the residue with tyrosine. Similarly, the Edmonston H protein did not bind CD46 when its Tyr481 was converted to asparagine. However, this mutation did not affect the ability of Edmonston H to bind marmoset and human B cells. The preceding results provide evidence, through the use of a direct binding assay, that a second receptor for measles virus is present on primate B cells.

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Section: Most Organs Of the Common Marmoset Contain Cd46 Molecules Wisupporting

confidence: 91%

Section: Most Organs Of the Common Marmoset Contain Cd46 Molecules Wisupporting

confidence: 49%

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confidence: 99%

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A Single Amino Acid Change in the Hemagglutinin Protein of Measles Virus Determines Its Ability To Bind CD46 and Reveals Another Receptor on Marmoset B Cells

Hsu

Sarangi

Iorio

et al. 1998

J Virol

144

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“…Results are expressed as means and standard deviations. mosets, tamarins, and squirrel monkeys (2,3,34). The disease in moustached marmosets has been reported to be characterized by severe gastroenterocolitis and immunosuppression (2), while the symptoms presented by squirrel monkeys are similar to those in humans and consist of a rash, Koplik's spots, and infection of lymphatic tissue (34).…”

Section: Discussionmentioning

confidence: 99%

Artificial mutations and natural variations in the CD46 molecules from human and monkey cells define regions important for measles virus binding

Hsu

Dörig

Sarangi

et al. 1997

J Virol

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CD46 was previously shown to be a primate-specific receptor for the Edmonston strain of measles virus. This receptor consists of four short consensus regions (SCR1 to SCR4) which normally function in complement regulation. Measles virus has recently been shown to interact with SCR1 and SCR2. In this study, receptors on different types of monkey erythrocytes were employed as "natural mutant proteins" to further define the virus binding regions of CD46. Erythrocytes from African green monkeys and rhesus macaques hemagglutinate in the presence of measles virus, while baboon erythrocytes were the least efficient of the Old World monkey cells used in these assays. Subsequent studies demonstrated that the SCR2 domain of baboon CD46 contained an Arg-to-Gln mutation at amino acid position 103 which accounted for reduced hemagglutination activity. Surprisingly, none of the New World monkey erythrocytes hemagglutinated in the presence of virus. Sequencing of cDNAs derived from the lymphocytes of these New World monkeys and analysis of their erythrocytes with SCR1-specific polyclonal antibodies indicated that the SCR1 domain was deleted in these cells. Additional experiments, which used 35 different site-specific mutations inserted into CD46, were performed to complement the preceding studies. The effects of these artificial mutations were documented with a convenient binding assay using insect cells expressing the measles virus hemagglutinin. Mutations which mimicked the change found in baboon CD46 or another which deleted the SCR2 glycosylation site reduced binding substantially. Another mutation which altered GluArg to AlaAla at positions 58 and 59, totally abolished binding. Finally, the epitopes for two monoclonal antibodies which inhibit measles virus attachment were mapped to the same regions implicated by mutagenesis.

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“…The maculopapular skin lesions are histologically characterized by focal hyperemia and hemorrhages in the lamina propria [64]. Experimental intracerebral inoculation of marmosets may cause encephalitis, which is similar to the subacute, sclerosing panencephalitis in humans [67,68]. Measles virus is strongly immunosuppressive, and the clinical picture may be complicated by secondary opportunistic viral or bacterial infections [67].…”

Section: Measles Virusmentioning

confidence: 99%