Abstract The coat of polyomavirus is composed of three proteins that can self-assemble to form an icosahedral capsid. VP1 represents 75% of the virus capsid protein and the VP1 capsomere subunits are capable of self assembly to form a capsid-like structure. Ground-based and orbiter studies were conducted with VP1 protein cloned in an expression vector and purified to provide ample quantities for capsomere-capsid assembly. Flight studies were conducted on STS-37 on April 5–9, 1991. Assembly initiated when a VP1 protein solution was interfaced with a Ca+2 buffer solution (pH 5.0). After four days a second alignment terminated the assembly process and allowed for glutaraldehyde fixation. Flight and ground-based samples were analyzed by electron microscopy. Ground-based experiments revealed the assembly of VP1 into capsid-like structures and a heterogenous size array of capsomere subunits. Samples reacted in microgravity, however, showed capsomeres of a homogenous size, but lack of capsid-like assembly.


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    Title :

    Virus protein assembly in microgravity


    Contributors:
    Chang, D. (author) / Paulsen, A. (author) / Johnson, T.C. (author) / Consigli, R.A. (author)

    Published in:

    Advances in Space Research ; 13 , 7 ; 251-257


    Publication date :

    1993-01-01


    Size :

    7 pages




    Type of media :

    Article (Journal)


    Type of material :

    Electronic Resource


    Language :

    English



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