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. Author manuscript; available in PMC: 2008 Nov 17.
Published in final edited form as: Biochem Biophys Res Commun. 2007 Jul 25;361(4):890–895. doi: 10.1016/j.bbrc.2007.07.086

Table 1.

Proposed oligomericity of Cry toxins

Oligomericity Toxin Experimental approach Dimensions Reference
Dimer Cry1Ab Incubating toxins with susceptible larval BBMVs1, analyzed by modified SDS-PAGE and Western blotting ∼ 130 kDa [35]
Dimer & Trimer Cry1Ac ∼ 130 kDa & ∼ 210 kDa
Dimer & Trimer Cry1Ac Using dynamics light scattering in buffer with different ionic strengths Molecular mass of each oligomer was derived from hydrodynamic radius of proteins from dynamics light scattering [36]
Trimer Cry1Aa,
Cry1Ab
Cry1Ac
Incubating toxins with susceptible larval BBMVs1, analyzed by modified SDS-PAGE and Western blotting ∼ 200 kDa [37,38]
Trimer Cry4Ba Incubating toxins with liposomes, analyzed by modified SDS-PAGE and Western blotting ∼ 200 kDa [30]
Tetramer Cry1Aa AFM2 of toxin inserted in bilayers in liquid cell Diameter 5 nm, each subunit 1.4 nm, depression 1.5 nm [21]
Tetramer Cry4Ba AFM2 of toxin inserted in bilayers in liquid cell Diameter 20-30 nm, height 2-4 nm [20]
Tetramer Cry1Ab ScFV73 cross-linked toxin3, binding with ANS 4 ∼ 250 kDa [19]
Large multimer Cry1Aa
Cry1Ac
Cry1Ca
Cry1D
Cry3Aa
Analyzed by native and modified SDS-PAGE, and size-exclusion chromatography >600 kDa [39]
1

BBMVs = Brush-border membrane vesicles

2

AFM = Atomic force microscopy

3

ScFV73 = A single chain antibody mimicking Bt-R1 receptor

4

ANS = 8-Anilino-1-naphthalenesulfonate