Crystal lattice as biological phenotype for insect viruses

• Published in: Protein science Vol. 14; no. 10; pp. 2741 - 2743
• Main Authors: Anduleit, Karin, Sutton, Geoff, Diprose, Jonathan M., Mertens, Peter P.C., Grimes, Jonathan M., Stuart, David I.
• Format: Journal Article
• Language: English
• Published: Bristol Cold Spring Harbor Laboratory Press 01.10.2005
• Subjects: Animals; Cell Line; crystals; For the Record; Inclusion Bodies, Viral - chemistry; Inclusion Bodies, Viral - metabolism; Insect Viruses - chemistry; Insect Viruses - physiology; insects; Intranuclear Inclusion Bodies - chemistry; Intranuclear Inclusion Bodies - metabolism; Moths - chemistry; Moths - virology; polyhedra; powder diffraction; Powder Diffraction - methods; Viral Structural Proteins - chemistry; Viral Structural Proteins - metabolism; viruses
• ISSN: 0961-8368; 1469-896X
• DOI: 10.1110/ps.051516405

Many insect viruses survive for long periods by occlusion within robust crystalline polyhedra composed primarily of a single polyhedrin protein. We show that two different virus families form polyhedra which, despite lack of sequence similarity in the virally encoded polyhedrin protein, have identical cell constants and a body‐centered cubic lattice. It is almost inconceivable that this could have arisen by chance, suggesting that the crystal lattice has been preserved because it is particularly well‐suited to its function of packaging and protecting viruses.