Solution Structure, Self-Assembly, and Membrane Interactions of the Matrix Protein from Newcastle Disease Virus at Neutral and Acidic pH

• DOI: 10.1128/jvi.01450-18
• Publication Date: 2018-12-19T10:55:51Z
• Authors: E. V. Shtykova; M. V. Petoukhov; L. A. Dadinova; N. V. Fedorova; V. Yu Tashkin; T. A. Timofeeva; A. L. Ksenofontov; N. A. Loshkarev; L. A. Baratova; C. M. Jeffries; D. I. Svergun; O. V. Batishchev
• Keywords: VP40; Mononegavirales; Newcastle Disease; Pneumovirinae

Newcastle disease virus (NDV) is an enveloped paramyxovirus. The matrix protein of the (M-NDV) has innate propensity to produce virus-like particles budding from plasma membrane expressing cell without recruiting other viral proteins. predominantly infects host via fusion with or, alternatively, can use receptor-mediated endocytic pathways. question arises as what are mechanisms supporting such diversity, especially concerning assembling and binding properties scaffold under both neutral acidic pH conditions. Here, we suggest a novel method M-NDV isolation in physiological ionic strength employ combination small-angle X-ray scattering, atomic force microscopy complementary structural techniques, interaction measurements characterize solution behavior/structure well its lipid membranes at 4.0 7.0. We demonstrate that minimal unit dimer spontaneously assembles milieu into hollow helical oligomers by repeating tetramers. Acidic conditions decrease oligomerization state individual dimers, tetramers, octamers changing density layer affinity, thus indicating pathway possible facilitator NDV entry through enhanced disintegration.