Structural Studies of the Ribonucleoprotein G-Antigen of Influenza Virus

1972 ◽  
Vol 27 (3) ◽  
pp. 246-251
Author(s):  
M. J. Sparks Levitch ◽  
Edward A. Eckert

The physical and serological states of ribonucleoprotein antigen, released by dissociation of influenza virus, have been characterized. While the simplest antigenic derivative has a sedimentation constant of 4s, more complex antigenic forms, 19s, 38s, and 60s have been identified and isolated. The physical dimensions of isolated g-antigen are dependent on the form of pretreatment of virus concentrate and on the method of virus disruption. The properties of several isolated substructures vary, depending on interaction of the protein with host antigen and nucleic acid.The results suggest that influenza virus ribonucleoprotein associates readily with host antigens and that this interaction plays a significant role in initiating the process of budding which leads to release of mature virus.

Nature ◽  
1955 ◽  
Vol 175 (4448) ◽  
pp. 209-210 ◽  
Author(s):  
G. L. ADA ◽  
BEVERLEY T. PERRY

1944 ◽  
Vol 79 (3) ◽  
pp. 267-283 ◽  
Author(s):  
W. M. Stanley

The sedimentation behavior of influenza virus in dilute solutions of electrolyte was found to be quite variable. At times the virus activity appeared to sediment at a rate comparable with that of particles about 80 to 120 mµ in diameter, at other times at a rate comparable with that of particles about 10 mµ in diameter, and at still other times the bulk of the activity appeared to sediment at a rate comparable with that of the larger particles and the residual activity at a rate comparable with that of the smaller particles. However, in the presence of a sucrose density gradient, the virus activity was always found to sediment with a rate comparable to that of particles about 80 to 120 mµ in diameter; hence it appeared that the variable sedimentation behavior in dilute electrolyte solution was due to convection or mechanical disturbances during centrifugation. About 30 per cent of the high molecular weight protein present in the allantoic fluid of chick embryos infected with the F 12 strain of influenza virus was found to consist of a component having a sedimentation constant of about 30 S, and hence a probable particle diameter of about 10 mµ. The residual protein of high molecular weight was present in the form of a component having a sedimentation constant of about 600 S, and hence a probable particle diameter of about 70 mµ. The proportion of the 30 S component in allantoic fluid of chick embryos infected with the PR8 strain of influenza virus was found to be considerably less. The 600 S and 30 S components of F 12 allantoic fluid were purified and separated by differential centrifugation. The purified preparations of the 600 S component were found to possess a specific virus activity from 100 to over 10,000 times that of the purified preparations of the 30 S component, the difference in activity apparently depending only on the degree of fractionation of the two components. The purified 30 S component was found to sediment normally in the presence of 12 per cent sucrose, whereas the small residual virus activity of such preparations was found to sediment in the presence of a sucrose density gradient with a rate comparable to that of much heavier particles. It is concluded that influenza virus activity is not associated with material having a particle diameter of about 10 mµ, but is associated solely with material having a sedimentation constant of about 600 S and hence a probable particle diameter of about 70 mµ.


2016 ◽  
Author(s):  
Nathan D. Thomsen ◽  
Michael R. Lawson ◽  
Lea B. Witkowsky ◽  
Song Qu ◽  
James M. Berger

ABSTRACTRing-shaped hexameric helicases and translocases support essential DNA, RNA, and protein-dependent transactions in all cells and many viruses. How such systems coordinate ATPase activity between multiple subunits to power conformational changes that drive the engagement and movement of client substrates is a fundamental question. Using the E. coli Rho transcription termination factor as a model system, we have employed solution and crystallographic structural methods to delineate the range of conformational changes that accompany distinct substrate and nucleotide cofactor binding events. SAXS data show that Rho preferentially adopts an open-ring state in solution, and that RNA and ATP are both required to cooperatively promote ring closure. Multiple closed-ring structures with different RNA substrates and nucleotide occupancies capture distinct catalytic intermediates accessed during translocation. Our data reveal how RNA-induced ring closure templates a sequential ATP-hydrolysis mechanism, provide a molecular rationale for how the Rho ATPase domains distinguishes between distinct RNA sequences, and establish the first structural snapshots of substepping events in a hexameric helicase/translocase.SIGNIFICANCEHexameric, ring-shaped translocases are molecular motors that convert the chemical energy of ATP hydrolysis into the physical movement of protein and nucleic acid substrates. Structural studies of several distinct hexameric translocases have provided insights into how substrates are loaded and translocated; however, the range of structural changes required for coupling ATP turnover to a full cycle of substrate loading and translocation has not been visualized for any one system. Here, we combine low-and high-resolution structural studies of the Rho helicase, defining for the first time the ensemble of conformational transitions required both for substrate loading in solution and for substrate movement by a processive hexameric translocase.


1989 ◽  
Vol 111 (3) ◽  
pp. 1082-1090 ◽  
Author(s):  
Ben Askew ◽  
Pablo Ballester ◽  
Chris Buhr ◽  
Kyu Sung Jeong ◽  
Sharon Jones ◽  
...  

Author(s):  
Jonathan P. Wong ◽  
Mary E. Christopher ◽  
Murray Cairns ◽  
L.-Q. Sun ◽  
Roderic M. K. Dale ◽  
...  

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