Helical structure of Bordetella pertussis fimbriae

Steven, Alasdair C.; Bisher, M. E.; Trus, Benes L.; Thomas, Daniel; Zhang, Jia Ming; Cowell, J L

doi:10.1128/jb.167.3.968-974.1986

Cited by 40 publications

(30 citation statements)

References 24 publications

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“…Certain amphiphilic nanoparticles (9), molecules (4,10,11), and some virus capsomers (12,13) that self-assemble into precise structures can, to first approximation, be modeled as cone-shaped particles associating via weak attractive interactions. What are the rules that govern the selfassembly of finite numbers of cones into precise clusters?…”

mentioning

confidence: 99%

A precise packing sequence for self-assembled convex structures

Chen¹,

Zhang²,

Glotzer

2007

Proc. Natl. Acad. Sci. U.S.A.

116

111

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Molecular simulations of the self-assembly of cone-shaped particles with specific, attractive interactions are performed. Upon cooling from random initial conditions, we find that the cones self-assemble into clusters and that clusters comprised of particular numbers of cones (e.g., 4 -17, 20, 27, 32, and 42) have a unique and precisely packed structure that is robust over a range of cone angles. These precise clusters form a sequence of structures at specific cluster sizes (a ''precise packing sequence'') that for small sizes is identical to that observed in evaporation-driven assembly of colloidal spheres. We further show that this sequence is reproduced and extended in simulations of two simple models of spheres self-assembling from random initial conditions subject to convexity constraints, including an initial spherical convexity constraint for moderate-and large-sized clusters. This sequence contains six of the most common virus capsid structures obtained in vivo, including large chiral clusters and a cluster that may correspond to several nonicosahedral, spherical virus capsids obtained in vivo. Our findings suggest that this precise packing sequence results from free energy minimization subject to convexity constraints and is applicable to a broad range of assembly processes.colloids ͉ self-assembly ͉ simulation ͉ virus assembly T he recent fabrication by means of evaporation-driven selfassembly of colloidal clusters containing micrometer-sized plastic spheres arranged in perfect polyhedra (1) has generated much excitement in the materials community. Precise structures such as these are rare in materials self-assembly problems (2, 3), with some notable, recent exceptions (e.g., refs. 4-6). In biology, however, precise structures are commonplace. A classic example is that of viruses, in which protein subunits, or small groups of protein subunits called capsomers, self-organize into precisely structured shells with icosahedral and other symmetries (7). Although obtained via wholly different processes, the precise packing of colloidal clusters [often referred to as colloidal ''molecules'' (8)] and virus capsids motivates us to investigate, in this article, the minimum set of organizing principles required for the self-assembly of precise structures such as these.One interesting building block shape that self-organizes into precise structures is the cone. Certain amphiphilic nanoparticles (9), molecules (4, 10, 11), and some virus capsomers (12, 13) that self-assemble into precise structures can, to first approximation, be modeled as cone-shaped particles associating via weak attractive interactions. What are the rules that govern the selfassembly of finite numbers of cones into precise clusters? Tsonchev et al. (14) presented a geometric packing analysis to explain the spherical shape resulting from the self-assembly of N cone-shaped amphiphilic nanoparticles in the limit of very large N, in which local hexagonal packing of hard cones is assumed. For clusters of smaller numbers of particles, however, the f...

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mentioning

confidence: 99%

A precise packing sequence for self-assembled convex structures

Chen¹,

Zhang²,

Glotzer

2007

Proc. Natl. Acad. Sci. U.S.A.

116

111

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“…Their diameter (4.5-5 nm) was smaller than that reported for the B . pertussis fimbriae (5-6 nm) studied by Steven et al (1986).…”

Section: Discussionmentioning

confidence: 99%

Immuno-electronmicroscopy of fimbriae-like structures on Bordetella pertussis serotype 1.3

Fredriksen¹,

Frøholm²

1988

Journal of Medical Microbiology

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Summary.Fimbriae-like filaments were demonstrated on the surface of Bordetella pertussis, serotype 1.3, by negative staining and electronmicroscopy. Immunoelectronmicroscopy with a monoclonal antibody specific for strains possessing agglutinogen 3, and colloidal gold, gave strong labelling of these structures. However, incubation with adsorbed polyclonal anti-agglutinogen 3 serum gave only weak labelling of the distal parts of the filaments and of the bacterial surface. The different binding patterns of the two antisera suggested that the epitopes involved were dissimilar. Thus, agglutinogen 3, as defined by conventional adsorbed sera, appeared to be associated with the fimbriae-like structures but was not necessarily identical to the fimbrial subunit protein. The monoclonal antibody, however, was more likely directed against the subunits of the fimbriae-like structures on serotype 1.3 bacteria.

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“…In the morphological analysis of the thin fimbriae of Bordetella pertussis, the subunits form a helical symmetry based on a single-start helix of 6.5 nm pitch with 2.5 repeating units per turn (25). From these parameters, the size of the subunit is calculated to be approximately 2.6 nm.…”

Section: Amino Acid Analysis Of the Us5 Fimbriaementioning

confidence: 99%

Antigenic Determinants on Fimbriae of Serratia marcescens US5 Analyzed Using Monoclonal Antibodies

Jingushi

Mitsuyama

Moriya

et al. 1987

Microbiology and Immunology

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The antigenic sites on small thin fimbriae of Serratia marcescens strain US5 were investigated using immunoelectron microscopy and monoclonal antibodies (MAbs). Negative staining of the fimbriae after treatment with MAbs showed a regularly spaced arrangement of the antibody molecules. When the subunit peptide was subjected to immunoblotting using the MAbs, a single band with a molecular weight of approximately 19kD was evident. This binding of the MAbs to the subunit peptide was completely abrogated after treatment with 2-mercaptoethanol, thereby suggesting the important role of disulfide linkage in the maintenance of the conformation of the antigenic site reacted with MAbs. Amino acid analysis of the subunit peptide revealed two cysteine residues, and cysteine residues were absent in the N-terminal portion.Bacterial fimbriae or pili are important virulent factors mediating adhesion of bacteria to the mucosal surface. Inhibition of the adherence by antibodies against fimbriae is an effective approach to prevent bacterial infection, in the early stage (17) .Chemical analyses of fimbriae showed that several different functional regions were involved (5,18,20,24). In the fimbriae of Neisseria gonorrheae, the region for adherence is located close to the antigenic site, and type-specific antibodies can effectively inhibit the adherence (24, 27). Morphologically, fimbriae can be grouped into two types, large thick fimbriae and small thin ones (13). Each fimbrial fiber consists of subunit peptides with a molecular weight of approximately 20,000 daltons. X-ray and optical diffraction studies revealed that the fimbrial fiber is formed by helical arrangement of subunits (7,8,27). Differences in the size of the fimbriae are mainly dependent on the mode of packing of the subunits, in a helical fashion (13). The relation of the structure and the functional regions of the fimbrial subunits has not been elucidated.Serratia marcescens causes nosocomial infections. We reported that S. marcescens strain US5 possessed mannose-sensitive fimbriae, that the adherence of this bacteria to the urinary bladder mucosal surface was mediated by small thin fimbriae, and that anti-fimbriae sera effectively inhibited the adherence (15,28). In the present 879

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Helical structure of Bordetella pertussis fimbriae

Cited by 40 publications

References 24 publications

A precise packing sequence for self-assembled convex structures

A precise packing sequence for self-assembled convex structures

Immuno-electronmicroscopy of fimbriae-like structures on Bordetella pertussis serotype 1.3

Antigenic Determinants on Fimbriae of Serratia marcescens US5 Analyzed Using Monoclonal Antibodies

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