Entomopoxviruses are a class of insect viruses whose virions are embedded in cytoplasmic occlusion bodies. The major component of these protective complexes is a protein called spheroidin/spindolin. Intermolecular disulphide bonds have been shown to play major roles in the formation and structure of these viral occlusion bodies [1] some of which are spindle body proteins.
Vaaje-Kolstad G, Houston DR, Riemen AH, Eijsink VG, van Aalten DM.
Crystal structure and binding properties of the Serratia marcescens chitin-binding protein CBP21.
J. Biol. Chem. 280 2005 11313-9
[PubMed: 15590674] http://dx.doi.org/10.1074/jbc.M407175200
Schnellmann J, Zeltins A, Blaak H, Schrempf H.
The novel lectin-like protein CHB1 is encoded by a chitin-inducible Streptomyces olivaceoviridis gene and binds specifically to crystalline alpha-chitin of fungi and other organisms.
Mol. Microbiol. 13 1994 807-19
[PubMed: 7815940] http://dx.doi.org/10.1111/j.1365-2958.1994.tb00473.x