Human Blood Group Influence on Reovirus Hemagglutination Titers

Brubaker, Margaret M.; West, Billy; Ellis, Robert J.

doi:10.3181/00379727-115-29130

Cited by 10 publications

(3 citation statements)

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“…The three feline isolates have hemagglutinating properties similar to those reported for reoviruses, particularly of human type III (2,4,9,17). Hemagglutinin titers were low.…”

Section: Resultssupporting

confidence: 56%

Characterization and Serotyping of Three Feline Reovirus Isolates

Csiza

1974

Infect Immun

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Three feline virus isolates were shown to be members of the reovirus group by their growth characteristics in cell cultures, physicochemical properties, and appearance under an electron microscope. Their close serological relationship to, or identity with, human reovirus type III was revealed by hemagglutination, hemagglutination inhibition, serum neutralization, and gel diffusion tests. One feline isolate (636) was pathogenic for suckling mice.

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“…The three feline isolates have hemagglutinating properties similar to those reported for reoviruses, particularly of human type III (2,4,9,17). Hemagglutinin titers were low.…”

Section: Resultssupporting

confidence: 56%

Characterization and Serotyping of Three Feline Reovirus Isolates

Csiza

1974

Infect Immun

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“…Chimeric 1 proteins display functional glycan-binding domains. Reovirus strains display serotype-specific patterns of hemagglutination (HA) as a consequence of binding to different sialic acid moieties on the surface of erythrocytes (22,(38)(39)(40)(41). The T1 glycan-binding site in the 1 head domain mediates agglutination of human erythrocytes (13), whereas sequences in the T3 1 head domain do not contribute to hemagglutination.…”

Section: Construction Of Chimeric 1 Reoviruses To Identify Protein Domentioning

confidence: 99%

Reovirus Neurotropism and Virulence Are Dictated by Sequences in the Head Domain of the Viral Attachment Protein

Sutherland

Aravamudhan

Dietrich

et al. 2018

J Virol

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Viral capsid components that bind cellular receptors mediate critical functions in viral tropism and disease pathogenesis. Mammalian orthoreoviruses (reoviruses) spread systemically in newborn mice to cause serotype-specific disease in the central nervous system (CNS). Serotype 1 (T1) reovirus infects ependymal cells to cause nonlethal hydrocephalus, whereas serotype 3 (T3) reovirus infects neurons to cause fulminant and lethal encephalitis. This serotype-dependent difference in tropism and concomitant disease is attributed to the σ1 viral attachment protein, which is composed of head, body, and tail domains. To identify σ1 sequences that contribute to tropism for specific cell types in the CNS, we engineered a panel of viruses expressing chimeric σ1 proteins in which discrete σ1 domains have been reciprocally exchanged. Parental and chimeric σ1 viruses were compared for replication, tropism, and disease induction following intracranial inoculation of newborn mice. Viruses expressing T1 σ1 head sequences infect the ependyma, produce relatively lower titers in the brain, and do not cause significant disease. In contrast, viruses expressing T3 σ1 head sequences efficiently infect neurons, replicate to relatively higher titers in the brain, and cause a lethal encephalitis. Additionally, T3 σ1 head-expressing viruses display enhanced infectivity of cultured primary cortical neurons compared with T1 σ1 head-expressing viruses. These results indicate that T3 σ1 head domain sequences promote infection of neurons, likely by interaction with a neuron-specific receptor, and dictate tropism in the CNS and induction of encephalitis. Viral encephalitis is a serious and often life-threatening inflammation of the brain. Mammalian orthoreoviruses are promising oncolytic therapeutics for humans but establish virulent, serotype-dependent disease in the central nervous system (CNS) of many young mammals. Serotype 1 reoviruses infect ependymal cells and produce hydrocephalus, whereas serotype 3 reoviruses infect neurons and cause encephalitis. Reovirus neurotropism is hypothesized to be dictated by the filamentous σ1 viral attachment protein. However, it is not apparent how this protein mediates disease. We discovered that sequences forming the most virion-distal domain of T1 and T3 σ1 coordinate infection of either ependyma or neurons, respectively, leading to mutually exclusive patterns of tropism and disease in the CNS. These studies contribute new knowledge about how reoviruses target cells for infection in the brain and inform the rational design of improved oncolytic therapies to mitigate difficult-to-treat tumors of the CNS.

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“…Type-specific HA has been observed with reoviruses; viruses of all three serotypes agglutinate human erythrocytes (1), and viruses of serotype 3 also agglutinate bovine erythrocytes (7). By using genetic reassortants derived from cells coinfected with type 1 and 3 reoviruses, it was shown that the S1 genome segment, which encodes outer capsid polypeptide crl, specified the virus hemagglutinin (31).…”

mentioning

confidence: 99%

Genetic reassortants for identification of the genome segment coding for the bluetongue virus hemagglutinin

Cowley¹,

Gorman²

1987

J Virol

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Two bluetongue virus (BTV) serotypes isolated in Australia and two selected reassortants derived from cells coinfected with these viruses have been used to identify the gene coding for the virus hemagglutinin. The parent viruses had characteristic hemagglutination patterns: BTV type 20 agglutinated sheep erythrocytes only; and BTV type 21 agglutinated sheep, bovine, human, and goose erythrocytes. Analysis of the two virus clones that had reassorted in genes coding for the outer capsid polypeptides demonstrated that hemagglutination and hemagglutination inhibition are functions associated with the outer capsid protein (VP2), which is encoded by genome segment 2.

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Human Blood Group Influence on Reovirus Hemagglutination Titers

Cited by 10 publications

References 0 publications

Characterization and Serotyping of Three Feline Reovirus Isolates

Characterization and Serotyping of Three Feline Reovirus Isolates

Reovirus Neurotropism and Virulence Are Dictated by Sequences in the Head Domain of the Viral Attachment Protein

Genetic reassortants for identification of the genome segment coding for the bluetongue virus hemagglutinin

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