Atomic-force-microscopy imaging and molecular-recognition-force microscopy of recrystallized heterotetramers comprising an S-layer-streptavidin fusion protein

被引:21
作者
Ebner, A
Kienberger, F
Huber, C
Kamruzzahan, ASM
Pastushenko, VP
Tang, JL
Kada, G
Gruber, HJ
Sleytr, UB
Sára, M
Hinterdorfer, P [1 ]
机构
[1] Univ Linz, Inst Biophys, A-4040 Linz, Austria
[2] Univ Nat Resources & Appl Life Sci, Ctr NanoBiotechnol, A-1180 Vienna, Austria
[3] Mol Imaging Corp, Tempe, AZ 85282 USA
关键词
AFM; imaging; nanoarrays; recognition; S-layers;
D O I
10.1002/cbic.200500445
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
S-layer proteins reassemble on surfaces to form 2D crystals with lattice constants in the nanometer range. By modifying these proteins with capture molecules through genetic engineering, specific binding sites, such as streptavidin tags, can be introduced. The activity of these sites is proven by single-molecule recognition-force spectroscopy. In addition, structural details of the morphological units were resolved by using dynamic force microscopy imaging. © 2006 Wiley-VCH Verlag GmbH & Co. KGaA.
引用
收藏
页码:588 / 591
页数:4
相关论文
共 39 条
[1]   Data analysis of interaction forces measured with the atomic force microscope [J].
Baumgartner, W ;
Hinterdorfer, P ;
Schindler, H .
ULTRAMICROSCOPY, 2000, 82 (1-4) :85-95
[2]   A novel approach to specific allergy treatment:: The recombinant fusion protein of a bacterial cell surface (S-layer) protein and the major birch pollen allergen Bet v 1 (rSbsC-Bet v 1) combines reduced allergenicity with immunomodulating capacity [J].
Bohle, B ;
Breitwieser, A ;
Zwölfer, B ;
Jahn-Schmid, B ;
Sára, M ;
Sleytr, UB ;
Ebner, C .
JOURNAL OF IMMUNOLOGY, 2004, 172 (11) :6642-6648
[3]   A recombinant bacterial cell surface (S-layer)-major birch pollen allergen-fusion protein (rSbsC/Bet v1) maintains the ability to self-assemble into regularly structured monomolecular lattices and the functionality of the allergen [J].
Breitwieser, A ;
Egelseer, EM ;
Moll, D ;
Ilk, N ;
Hotzy, C ;
Bohle, B ;
Ebner, C ;
Sleytr, UB ;
Sára, M .
PROTEIN ENGINEERING, 2002, 15 (03) :243-249
[4]  
De Paris R., 2000, Single Molecules, V1, P285
[5]   Localization of single avidin-biotin interactions using simultaneous topography and molecular recognition imaging [J].
Ebner, A ;
Kienberger, F ;
Kada, G ;
Stroh, CM ;
Geretschläger, M ;
Kamruzzahan, ASM ;
Wildling, L ;
Johnson, WT ;
Ashcroft, B ;
Nelson, J ;
Lindsay, SM ;
Gruber, HJ ;
Hinterdorfer, P .
CHEMPHYSCHEM, 2005, 6 (05) :897-900
[6]   Structural research on surface layers: A focus on stability, surface layer homology domains, and surface layer cell wall interactions [J].
Engelhardt, H ;
Peters, J .
JOURNAL OF STRUCTURAL BIOLOGY, 1998, 124 (2-3) :276-302
[7]   Imaging and manipulation of biological structures with the AFM [J].
Fotiadis, D ;
Scheuring, S ;
Müller, SA ;
Engel, A ;
Müller, DJ .
MICRON, 2002, 33 (04) :385-397
[8]   New approaches to nanofabrication: Molding, printing, and other techniques [J].
Gates, BD ;
Xu, QB ;
Stewart, M ;
Ryan, D ;
Willson, CG ;
Whitesides, GM .
CHEMICAL REVIEWS, 2005, 105 (04) :1171-1196
[9]   The evolution of dip-pen nanolithography [J].
Ginger, DS ;
Zhang, H ;
Mirkin, CA .
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, 2004, 43 (01) :30-45
[10]  
GOULD P., 2003, MATER TODAY, V6, P34