A dominant temperature-sensitive assembly mutant of adenovirus type 2

1979 ◽  
Vol 25 (5) ◽  
pp. 646-649 ◽  
Author(s):  
Eric B. Carstens ◽  
Johanne Magnan ◽  
Joseph Weber
Keyword(s):  
Negative Temperature ◽  
Adenovirus Type ◽  
Wild Type Virus ◽  
Temperature Sensitive ◽  
Nonpermissive Temperature ◽  
Wild Type ◽  
Sensitive Mutant ◽  
Virion Assembly ◽  
Temperature Sensitive Mutant

An assembly negative temperature-sensitive mutant of Ad2, ts48 was shown to exert dominance over other ts mutants and wild-type virus during coinfection, by inhibiting virion assembly. Dominance was only expressed at the nonpermissive temperature.

Biological and Structural Studies with an Adenovirus Type 2 Temperature-Sensitive Mutant Defective for Uncoating

Intervirology ◽  
1983 ◽  
Vol 19 (4) ◽  
pp. 213-223 ◽  
Author(s):  
Charles Hannan ◽  
Leda H. Raptis ◽  
Claude V. Déry ◽  
Joseph Weber
Keyword(s):  
Adenovirus Type ◽  
Temperature Sensitive ◽  
Structural Studies ◽  
Sensitive Mutant ◽  
Temperature Sensitive Mutant ◽  
Adenovirus Type 2

scholarly journals Cryo-Electron Microscopy Structure of Adenovirus Type 2 Temperature-Sensitive Mutant 1 Reveals Insight into the Cell Entry Defect

2009 ◽  
Vol 83 (15) ◽  
pp. 7375-7383 ◽  
Author(s):  
Mariena Silvestry ◽  
Steffen Lindert ◽  
Jason G. Smith ◽  
Oana Maier ◽  
Christopher M. Wiethoff ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Adenovirus Type ◽  
Cell Entry ◽  
Temperature Sensitive ◽  
Sensitive Mutant ◽  
Temperature Sensitive Mutant ◽  
The Core ◽  
Cryo Electron Microscopy ◽  
Adenovirus Type 2

ABSTRACT The structure of the adenovirus type 2 temperature-sensitive mutant 1 (Ad2ts1) was determined to a resolution of 10 Å by cryo-electron microscopy single-particle reconstruction. Ad2ts1 was prepared at a nonpermissive temperature and contains the precursor forms of the capsid proteins IIIa, VI, and VIII; the core proteins VII, X (mu), and terminal protein (TP); and the L1-52K protein. Cell entry studies have shown that although Ad2ts1 can bind the coxsackievirus and Ad receptor and undergo internalization via αv integrins, this mutant does not escape from the early endosome and is targeted for degradation. Comparison of the Ad2ts1 structure to that of mature Ad indicates that Ad2ts1 has a different core architecture. The Ad2ts1 core is closely associated with the icosahedral capsid, a connection which may be mediated by preproteins IIIa and VI. Density within hexon cavities is assigned to preprotein VI, and membrane disruption assays show that hexon shields the lytic activity of both the mature and precursor forms of protein VI. The internal surface of the penton base in Ad2ts1 appears to be anchored to the core by interactions with preprotein IIIa. Our structural analyses suggest that these connections to the core inhibit the release of the vertex proteins and lead to the cell entry defect of Ad2ts1.

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