2k48

Publication Abstract from PubMed

The hantaviruses are emerging infectious viruses that in humans can cause a cardiopulmonary syndrome or a hemorrhagic fever with renal syndrome. The nucleocapsid (N) is the most abundant viral protein, and during viral assembly, the N protein forms trimers and packages the viral RNA genome. Here, we report the NMR structure of the N-terminal domain (residues 1-74, called N1-74) of the Andes hantavirus N protein. N1-74 forms two long helices (alpha1 and alpha2) that intertwine into a coiled coil domain. The conserved hydrophobic residues at the helix alpha1-alpha2 interface stabilize the coiled coil; however, there are many conserved surface residues whose function is not known. Site-directed mutagenesis, CD spectroscopy, and immunocytochemistry reveal that a point mutation in the conserved basic surface formed by Arg22 or Lys26 lead to antibody recognition based on the subcellular localization of the N protein. Thus, Arg22 and Lys26 are likely involved in a conformational change or molecular recognition when the N protein is trafficked from the cytoplasm to the Golgi, the site of viral assembly and maturation.

NMR structure of the N-terminal coiled coil domain of the Andes hantavirus nucleocapsid protein.,Wang Y, Boudreaux DM, Estrada DF, Egan CW, St Jeor SC, De Guzman RN J Biol Chem. 2008 Oct 17;283(42):28297-304. Epub 2008 Aug 7. PMID:18687679^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.