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Microtubule-associated protein 2 appears in axons of cultured dorsal root ganglia and spinal cord neurons after rotavirus infection.

Artikel i vetenskaplig tidskrift
Författare K Weclewicz
L Svensson
Martin Billger
K Holmberg
Margareta Wallin
K Kristensson
Publicerad i Journal of neuroscience research
Volym 36
Nummer/häfte 2
Sidor 173-82
ISSN 0360-4012
Publiceringsår 1993
Publicerad vid Zoologiska institutionen
Sidor 173-82
Språk en
Länkar dx.doi.org/10.1002/jnr.490360207
Ämnesord Animals, Axons, metabolism, Cattle, Cells, Cultured, Cytoskeleton, metabolism, Enzyme-Linked Immunosorbent Assay, Female, Ganglia, Spinal, cytology, metabolism, Immunohistochemistry, Microtubule-Associated Proteins, metabolism, Neurons, metabolism, Pregnancy, RNA, Viral, biosynthesis, Rats, Rats, Sprague-Dawley, Rotavirus Infections, metabolism, Spinal Cord, cytology, metabolism, Viral Proteins, biosynthesis, Virus Replication, tau Proteins, metabolism
Ämneskategorier Cell- och molekylärbiologi

Sammanfattning

The immunohistochemical distribution of microtubule-associated protein 2 (MAP2), being normally restricted to nerve cell bodies and dendrites, became altered in rat dorsal root ganglia and spinal cord neurons in cultures infected with rhesus rotavirus. MAP2 appeared in axons of both sources of neurons as displayed with monoclonal antibodies to MAP2a + b and MAP2a + b + c at 48 hr post-infection (p.i.). Other cytoskeletal elements, i.e., tau, MAP1, MAP5, neurofilament, actin, and tubulin, did not reveal any alterations in the rotavirus-infected neurons. One of the rotavirus cytosolic proteins, the inner capsid protein vp6, was expressed in axons at 48 hr p.i. simultaneously with the appearance of MAP2, while two other viral proteins, vp4 and NS28, remained in the nerve cell bodies. By quantitative enzyme-linked immunosorbent assay (ELISA) a binding of single-shelled rotaviruses, which express vp6 on their surfaces, to purified MAP2 was found. There was no binding of these viral particles to tau or tubulin proteins. This study indicates that a selective interaction between certain viral and neuronal cytoskeletal proteins can occur and that a non-cytolytic viral infection can cause alterations in the polarized sorting of neuronal proteins.

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