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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
Gene Review

M  -  membrane protein

Human coronavirus OC43

 
 
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Disease relevance of M

 

High impact information on M

  • Thus, the S protein, which on itself was transported to the plasma membrane, was retained in the Golgi complex by its association with the M protein [6].
  • Complementary biochemical experiments were carried out to determine whether vesicular transport was required for the newly synthesized M protein, that contains only O-linked oligosaccharides, to acquire first, GalNAc and second, the Golgi modifications galactose and sialic acid [7].
  • The results from both in vivo studies and from the use of SLO-permeabilized cells showed that, while GalNAc addition occurred under conditions which block vesicular transport, both cytosol and ATP were prerequisites for the M protein oligosaccharides to acquire Golgi modifications [7].
  • Moreover, a mutant of the M protein lacking the 22 COOH-terminal amino acids, that is transported to the plasma membrane, gave rise to similar complexes, albeit smaller in size, that persisted at the plasma membrane [8].
  • Using pulse-chase analyses we studied the oligomerization of the M protein in sucrose gradients [8].
 

Chemical compound and disease context of M

 

Biological context of M

 

Anatomical context of M

 

Associations of M with chemical compounds

  • In contrast, folding and transport of the M protein were not inhibited by DTT [18].
 

Physical interactions of M

  • Pulse-labeling experiments showed that newly synthesized, unglycosylated M protein interacted with N protein in a pre-Golgi compartment, which is part of the MHV budding site [10].
 

Other interactions of M

  • Analysis of second-site revertants of MDelta2 revealed mutations in the carboxy-terminal region of the N protein that compensated for the defect in the M protein [1].
  • Epitopes inducing protective humoral responses to virus infection were located mainly in the M protein and a region spanning residues 13-877 of the S protein [19].

References

  1. A major determinant for membrane protein interaction localizes to the carboxy-terminal domain of the mouse coronavirus nucleocapsid protein. Hurst, K.R., Kuo, L., Koetzner, C.A., Ye, R., Hsue, B., Masters, P.S. J. Virol. (2005) [Pubmed]
  2. Cooperation of an RNA packaging signal and a viral envelope protein in coronavirus RNA packaging. Narayanan, K., Makino, S. J. Virol. (2001) [Pubmed]
  3. Genetic evidence for a structural interaction between the carboxy termini of the membrane and nucleocapsid proteins of mouse hepatitis virus. Kuo, L., Masters, P.S. J. Virol. (2002) [Pubmed]
  4. Glycosylation of the severe acute respiratory syndrome coronavirus triple-spanning membrane proteins 3a and M. Oostra, M., de Haan, C.A., de Groot, R.J., Rottier, P.J. J. Virol. (2006) [Pubmed]
  5. Immune response to a murine coronavirus: identification of a homing receptor-negative CD4+ T cell subset that responds to viral glycoproteins. Mobley, J., Evans, G., Dailey, M.O., Perlman, S. Virology (1992) [Pubmed]
  6. Envelope glycoprotein interactions in coronavirus assembly. Opstelten, D.J., Raamsman, M.J., Wolfs, K., Horzinek, M.C., Rottier, P.J. J. Cell Biol. (1995) [Pubmed]
  7. Characterization of the budding compartment of mouse hepatitis virus: evidence that transport from the RER to the Golgi complex requires only one vesicular transport step. Krijnse-Locker, J., Ericsson, M., Rottier, P.J., Griffiths, G. J. Cell Biol. (1994) [Pubmed]
  8. Oligomerization of a trans-Golgi/trans-Golgi network retained protein occurs in the Golgi complex and may be part of its retention. Locker, J.K., Opstelten, D.J., Ericsson, M., Horzinek, M.C., Rottier, P.J. J. Biol. Chem. (1995) [Pubmed]
  9. Assembly of spikes into coronavirus particles is mediated by the carboxy-terminal domain of the spike protein. Godeke, G.J., de Haan, C.A., Rossen, J.W., Vennema, H., Rottier, P.J. J. Virol. (2000) [Pubmed]
  10. Characterization of the coronavirus M protein and nucleocapsid interaction in infected cells. Narayanan, K., Maeda, A., Maeda, J., Makino, S. J. Virol. (2000) [Pubmed]
  11. Accelerated induction of apoptosis in insect cells by baculovirus-expressed SARS-CoV membrane protein. Lai, C.W., Chan, Z.R., Yang, D.G., Lo, W.H., Lai, Y.K., Chang, M.D., Hu, Y.C. FEBS Lett. (2006) [Pubmed]
  12. The glycosylation status of the murine hepatitis coronavirus M protein affects the interferogenic capacity of the virus in vitro and its ability to replicate in the liver but not the brain. de Haan, C.A., de Wit, M., Kuo, L., Montalto-Morrison, C., Haagmans, B.L., Weiss, S.R., Masters, P.S., Rottier, P.J. Virology (2003) [Pubmed]
  13. The amino-terminal signal peptide on the porcine transmissible gastroenteritis coronavirus matrix protein is not an absolute requirement for membrane translocation and glycosylation. Kapke, P.A., Tung, F.Y., Hogue, B.G., Brian, D.A., Woods, R.D., Wesley, R. Virology (1988) [Pubmed]
  14. Genetic manipulation of equine arteritis virus using full-length cDNA clones: separation of overlapping genes and expression of a foreign epitope. de Vries, A.A., Glaser, A.L., Raamsman, M.J., de Haan, C.A., Sarnataro, S., Godeke, G.J., Rottier, P.J. Virology (2000) [Pubmed]
  15. Identification of a CD4+ T cell epitope within the M protein of a neurotropic coronavirus. Xue, S., Jaszewski, A., Perlman, S. Virology (1995) [Pubmed]
  16. Mutations in Sendai virus variant F1-R that correlate with plaque formation in the absence of trypsin. Hou, X., Suquilanda, E., Zeledon, A., Kacsinta, A., Moore, A., Seto, J., McQueen, N. Med. Microbiol. Immunol. (Berl.) (2005) [Pubmed]
  17. Coronavirus immunogens. Saif, L.J. Vet. Microbiol. (1993) [Pubmed]
  18. Disulfide bonds in folding and transport of mouse hepatitis coronavirus glycoproteins. Opstelten, D.J., de Groote, P., Horzinek, M.C., Vennema, H., Rottier, P.J. J. Virol. (1993) [Pubmed]
  19. Protective humoral responses to severe acute respiratory syndrome-associated coronavirus: implications for the design of an effective protein-based vaccine. Pang, H., Liu, Y., Han, X., Xu, Y., Jiang, F., Wu, D., Kong, X., Bartlam, M., Rao, Z. J. Gen. Virol. (2004) [Pubmed]
 
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