STUDY OF VIRUS PROTEIN REPOLYMERIZATION AND RECONSTRUCTION OF SOME ROD- LIKE VIRUSES

• Main Authors: Kiselev, N A, Atabekov, I G, Kaftanova, A S, Novikov, V K
• Format: Report
• Language: English
• Subjects: Biochemistry; DEGRADATION; FOREIGN REPORTS; Microbiology; MOLECULAR STRUCTURE; MORPHOLOGY(BIOLOGY); POLYMERIZATION; PROTEINS; RIBONUCLEIC ACIDS; SEDIMENTATION; TRANSLATIONS; USSR; VIRUSES

Products formed by the degradation of barley stripe mosaic virus (BSMV) were investigated by various methods. The protein subunit of this virus is characterized by a sedimentation constant of 1.8S. The subunits are capable of aggregating, forming particles with 12, 25S (discs) and higher sedimentation coefficients (disc piles and helical structures). An investigation was made of the dependency of repolymerization of BSMV virus on the conditions (molarity of the buffer, pH, temperature) and the method of degradation. Two main types of specific aggregates were formed during the repolymerization of BSMV protein: Structures with a helical arrangement of subunits and structures characterized by a rotational symmetry (discs, paired discs and rod-like aggregates formed from discs) The protein capsule of BSMV contains 1130--1140 subunits with a molecular weight of 22000M forming around 50 turns. Approximately 24 subunits are included in the disc-shaped structures. The protein of cucumber mosaic virus No 2 (CMV-2) is characterized by a clearly expressed tendency for repolymerization, which it is capable of carrying out even under those conditions (pH 8.5) when the repolymerization of TMV and BSMV cannot take place. The main product of CMV-2 repolymerization are helical structures. In the experiments with TMV and BSMV it was demonstrated that in the presence of RNA the reconstitution of helical structures occurs under those conditions when repolymerization cannot be accomplished. Trans. of Biokhimiya (USSR) v31 n4 p670-8 1966.