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Chapter 4 : Adhesins as Bacterial Cell Surface Structures: General Concepts of Structure, Biogenesis, and Regulation

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Abstract:

This chapter presents concise reviews of the general architectural plan of gram-positive and gram-negative cell surfaces. Within this context, a few specific examples are used to present basic concepts of the genetics of adhesin expression and adhesive organelle biogenesis. The adhesins of the gram-positive bacteria are anchored on the surface by four different mechanisms that include cell wall-anchoring mechanism, transmembrane mechanism, association of adhesins with surface proteins and the association of adhesins with surface glycolipids. The best described and probably the most prominent mechanism for anchoring adhesins is the cell wall-anchoring mechanism. The adhesins of the gram-negative bacteria are anchored on the outer membrane surface by four different mechanisms. The most widely used mechanism for fimbrial biogenesis appears to be the chaperone-usher pathway. This pathway is shared by many enterobacteria as well as some respiratory pathogens. Expression of type 1 fimbriae, as well as several other virulence factors, can also be affected in certain strains of by the excision of pathogenicity islands. Short peptides that inhibit quorumsensing mechanisms were found to inhibit adhesion to epithelial cells as well as biofilm formation on medical device plastics. This is an interesting and promising new direction in the efforts to develop antiadhesion therapies for infectious diseases.

Citation: Ofek I, Hasty D, Doyle R. 2003. Adhesins as Bacterial Cell Surface Structures: General Concepts of Structure, Biogenesis, and Regulation, p 63-96. In Bacterial Adhesion to Animal Cells and Tissues. ASM Press, Washington, DC. doi: 10.1128/9781555817800.ch4

Key Concept Ranking

Bacterial Proteins
0.6912605
Bacterial Cell Structure
0.56265855
Type 1 Fimbriae
0.53562987
Bacterial Virulence Factors
0.52605695
Outer Membrane Proteins
0.4956032
0.6912605
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Image of FIGURE 4.1
FIGURE 4.1

Schematic representation of the cell surface of a gram-positive bacterium. External to the cytoplasmic membrane is a multilayered peptidoglycan matrix composed of acetylglucosamine (GEOMETRIC SHAPE) and -acetylmuramic acid (GEOMETRIC SHAPE). Many surface proteins are covalently anchored to muramic acid (see Fig. 4.3 ) but extend through the peptidoglycan to be presented at the bacterial surface. Adhesion functions may be ascribed to virtually any surface structure or macromolecule. In electron micrographs, the most prominent adhesins appear to be in the form of fibrils and filamentous structures. Lipoteichoic acid can be found within the cytoplasmic membrane but is also secreted through the cell wall and surface protein layer, often becoming associated with proteins and reoriented to contribute to the hydrophobic characteristics of the cell surface.

Citation: Ofek I, Hasty D, Doyle R. 2003. Adhesins as Bacterial Cell Surface Structures: General Concepts of Structure, Biogenesis, and Regulation, p 63-96. In Bacterial Adhesion to Animal Cells and Tissues. ASM Press, Washington, DC. doi: 10.1128/9781555817800.ch4
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Image of FIGURE 4.2
FIGURE 4.2

Schematic representation of the cell surface of a gram-negative bacterium. External to the cytoplasmic membrane is a periplasmic space, a few layers of peptidoglycan matrix, and an outer membrane in which adhesins are embedded. Gram-negative bacterial adhesins are most often found on fimbriae, although fibrils, flagella, OMPs, and capsule can also possess adhesin characteristics. The adhesive subunit of fimbriae may be found at the fimbrial tips (illustrated) or at multiple sites along the length (not illustrated). In most cases, adhesins are integral components of the outer membrane, but examples of secreted components that become associated with integral membrane components do exist.

Citation: Ofek I, Hasty D, Doyle R. 2003. Adhesins as Bacterial Cell Surface Structures: General Concepts of Structure, Biogenesis, and Regulation, p 63-96. In Bacterial Adhesion to Animal Cells and Tissues. ASM Press, Washington, DC. doi: 10.1128/9781555817800.ch4
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Image of FIGURE 4.3
FIGURE 4.3

Hypothetical model for the anchorage of surface proteins to cell wall peptidoglycan. The process is divided into four steps. In step 1, the full-length precursor of a surface protein is exported via an N-terminal leader peptide; in step 2, the protein is prevented from being released extracellularly by a hydrophobic membrane-spanning domain and a charged cytoplasmic tail; in step 3, the protein is cleaved between Thr and Gly of the LPXTG motif by the sortase enzyme; and in step 4, the newly cleaved carboxy terminus of Thr is linked to the amino group at the end of a cell wall cross-bridging peptide. (Reprinted from reference with permission from the publisher.)

Citation: Ofek I, Hasty D, Doyle R. 2003. Adhesins as Bacterial Cell Surface Structures: General Concepts of Structure, Biogenesis, and Regulation, p 63-96. In Bacterial Adhesion to Animal Cells and Tissues. ASM Press, Washington, DC. doi: 10.1128/9781555817800.ch4
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Image of FIGURE 4.4
FIGURE 4.4

Schematic diagrams of wall teichoic acid (A) and membrane lipoteichoic acid (B) contained in the cell walls of gram-positive organisms. Teichoic acid is composed primarily of repeating glycerol-phosphate units linked via a saccharide moiety to -acetylmuramic acid (MurNAc). The numbers of glycerol-phosphate units, the substitutions of glycerol (not shown), and the specific structure of the saccharide linkage moiety are species specific. Lipoteichoic acid is similar, in that a poly-glycerol-phosphate chain is linked via a saccharide moiety to its anchor. In this case, however, the anchor is not peptidoglycan but, instead, consists of fatty acid moieties that are embedded in the outer half of the cytoplasmic membrane.

Citation: Ofek I, Hasty D, Doyle R. 2003. Adhesins as Bacterial Cell Surface Structures: General Concepts of Structure, Biogenesis, and Regulation, p 63-96. In Bacterial Adhesion to Animal Cells and Tissues. ASM Press, Washington, DC. doi: 10.1128/9781555817800.ch4
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Image of FIGURE 4.5
FIGURE 4.5

Schematic illustration of features common to many wall-anchored surface proteins. All feature an N-terminal leader sequence followed by regions either without (open areas) or with (hatched areas) repeating domains, an LPXTG sorting signal, and a charged C-terminal cytoplasmic tail. Some proteins contain a dozen or more repeated domains, and the number of repeats of the proteins expressed by different clones within one species is often variable. In some cases, proline-rich areas are present distal to the LPXTG motif and may aid the protein in traversing the thick peptidoglycan layer.

Citation: Ofek I, Hasty D, Doyle R. 2003. Adhesins as Bacterial Cell Surface Structures: General Concepts of Structure, Biogenesis, and Regulation, p 63-96. In Bacterial Adhesion to Animal Cells and Tissues. ASM Press, Washington, DC. doi: 10.1128/9781555817800.ch4
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Image of FIGURE 4.6
FIGURE 4.6

Schematic illustration of the elastin binding surface protein, EbpS. This is an example of a surface protein that is not anchored via an LPXTG motif and sortase enzyme but, instead, is anchored via two or three hydrophobic domains thought to be oriented in one of two possible ways with regard to the cytoplasmic membrane. (Reprinted from reference with permission from the publisher.)

Citation: Ofek I, Hasty D, Doyle R. 2003. Adhesins as Bacterial Cell Surface Structures: General Concepts of Structure, Biogenesis, and Regulation, p 63-96. In Bacterial Adhesion to Animal Cells and Tissues. ASM Press, Washington, DC. doi: 10.1128/9781555817800.ch4
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Image of FIGURE 4.7
FIGURE 4.7

Electron micrographs of , illustrating surface fuzz. Streptococci were grown overnight in broth and then incubated in the absence (A) or presence (B) of plasma. binds several different serum and plasma proteins (e.g. fibrinogen, fibronectin, and albumin), which dramatically accentuate the presence of surface fibrils. Magnification, ×75,000.

Citation: Ofek I, Hasty D, Doyle R. 2003. Adhesins as Bacterial Cell Surface Structures: General Concepts of Structure, Biogenesis, and Regulation, p 63-96. In Bacterial Adhesion to Animal Cells and Tissues. ASM Press, Washington, DC. doi: 10.1128/9781555817800.ch4
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Image of FIGURE 4.8
FIGURE 4.8

Differing morphologies of structures on the surfaces of oral streptococci. (A) A dividing cell of strain GW2 negatively stained with 1% (wt/vol) methylamine tungstate. A dense fringe of peritrichous, short fibrils (75.3 ± 22 nm long) is visible, but no fibrils can yet be seen on the newly developing cell wall near the septum. (B) CN 3410 stained with 1% methylamine tungstate. One side of the cell carries a dense tuft of fibrils of two lengths. Longer, sparser fibrils (289 ± 15 nm long) project through a very dense fringe of shorter tuft fibrils (159 ± 5 nm long). An indistinct fuzz covers the rest of the cell surface. Magnifications: ×73,500 (A) and ×85,700 (B). Micrographs were provided courtesy of Pauline Handley.

Citation: Ofek I, Hasty D, Doyle R. 2003. Adhesins as Bacterial Cell Surface Structures: General Concepts of Structure, Biogenesis, and Regulation, p 63-96. In Bacterial Adhesion to Animal Cells and Tissues. ASM Press, Washington, DC. doi: 10.1128/9781555817800.ch4
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Image of FIGURE 4.9
FIGURE 4.9

Schematic diagrams illustrating the orchestration of adhesin and secreted toxin expression across the growth curve and regulatory mechanisms. (A) Schematic illustration of the early log, mid-log, late log, and stationary phases of the growth curve, in relation to the expression of adhesins, the transcription “effector” RNAIII, and secreted toxins. Adhesins begin to be expressed in early-log phase, peak by mid-log phase, and begin to be turned off by late-log phase by the expression of the locus and the RNAIII effector. (B) Schematic illustration of the Agr and RAP-TRAP quorum-sensing transcripton regulation systems of As the cell density increases, the levels of the autoinducing molecules AIP and RAP reach a threshold and activate the expression of AgrB and AgrD combine to express and secrete AIP, which binds to the sensor protein AgrC. AgrC is phosphorylated, and the phosphate group is transferred to the response regulator AgrA, which activates the transcription of RNAII and RNAIII. RNAII encodes an additional autoinducing peptide, sensor, and response regulator, while RNAIII is the primary activator or suppressor of transcription of multiple targets. (Panel A modified from reference .)

Citation: Ofek I, Hasty D, Doyle R. 2003. Adhesins as Bacterial Cell Surface Structures: General Concepts of Structure, Biogenesis, and Regulation, p 63-96. In Bacterial Adhesion to Animal Cells and Tissues. ASM Press, Washington, DC. doi: 10.1128/9781555817800.ch4
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Image of FIGURE 4.10
FIGURE 4.10

Schematic illustration of several different regulatory systems. The locus was the first described virulence factor regulon and remains the best characterized. Mga is a DNA binding protein that activates the transcription of a number of surface proteins, some of which are known to serve as adhesins. Mga is self-regulating and is suppressed by Nra and RofA. The FasBCAX locus upregulates a fibronectin binding adhesin, Fbp54, and Mrp. FasB and FasC appear to serve as sensor molecules, with FasA being the response regulator. The transcript does not encode a protein but serves as a regulatory RNA molecule. Thus, the locus has some similarities to the locus. CovR/CovS (also CsrRS) is another two-component regulatory system in which CovS is the membrane-bound sensor molecule and CovR is the response regulator. Recent evidence suggest that this global regulatory system affects up to 15% of the genome.

Citation: Ofek I, Hasty D, Doyle R. 2003. Adhesins as Bacterial Cell Surface Structures: General Concepts of Structure, Biogenesis, and Regulation, p 63-96. In Bacterial Adhesion to Animal Cells and Tissues. ASM Press, Washington, DC. doi: 10.1128/9781555817800.ch4
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Image of FIGURE 4.11
FIGURE 4.11

Electron micrograph of a negatively stained recombinant strain expressing type 1 fimbriae. These fimbriae and others of its class are peritrichously arranged, can number in the hundreds per cell, and are rigid, straight structures. There are 1,000 or more FimA subunits polymerized into a 7-nm-diameter helical structure. This subunit makes up the majority of the fimbrial structure. The mannose binding lectin, FimH, is located at the distal tip of the fimbriae. Magnification, ×28,615.

Citation: Ofek I, Hasty D, Doyle R. 2003. Adhesins as Bacterial Cell Surface Structures: General Concepts of Structure, Biogenesis, and Regulation, p 63-96. In Bacterial Adhesion to Animal Cells and Tissues. ASM Press, Washington, DC. doi: 10.1128/9781555817800.ch4
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Image of FIGURE 4.12
FIGURE 4.12

Electron micrographs illustrating the capsule. Bacteria were grown on lactose-supplemented medium, harvested, and incubated overnight at 4°C with preimmune serum or anticapsule serum. After fixation and staining with ruthenium red, the bacteria were processed for thin sectioning. (A) Without antibody stabilization, the capsular material contracts during processing and is barely visible. (B) With antibody stabilization, the extent of the capsule is clearly indicated. Magnification, ×45,000.

Citation: Ofek I, Hasty D, Doyle R. 2003. Adhesins as Bacterial Cell Surface Structures: General Concepts of Structure, Biogenesis, and Regulation, p 63-96. In Bacterial Adhesion to Animal Cells and Tissues. ASM Press, Washington, DC. doi: 10.1128/9781555817800.ch4
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Image of FIGURE 4.13
FIGURE 4.13

Electron micrograph of a negatively stained preparation of purified type 1 fimbriae. Their rigid structures are even more evident than in a micrograph of an intact bacterium. Magnification, ×39,375.

Citation: Ofek I, Hasty D, Doyle R. 2003. Adhesins as Bacterial Cell Surface Structures: General Concepts of Structure, Biogenesis, and Regulation, p 63-96. In Bacterial Adhesion to Animal Cells and Tissues. ASM Press, Washington, DC. doi: 10.1128/9781555817800.ch4
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Image of FIGURE 4.14
FIGURE 4.14

Electron micrograph of a P-fimbriated cell. (A) recombinant cell possessing the pPAP5 plasmid, which contains the entire P fimbrial gene cluster, was fixed first with glutaraldehyde and then with osmium tetroxide and allowed to attach to freshly cleaved mica. The samples were dried, rotary shadowed with platinum and carbon, and viewed under a transmission electron microscope. The main 7-nm shafts of the heteropolymeric fimbriae extend individually from the surface of the bacterium, although sometimes they lie so closely that they appear to form bundles. Tip fibrillae typical of this class of fimbriae extend from the distal ends of several fimbriae (arrowheads). The diameter of the tip fibrillum is roughly half the diameter of the main shaft and is composed of the PapG adhesin subunit at the tips bound to several PapE subunits and finally to a PapK subunit to anchor the fibrillum to the PapA subunits that make up the primary 7-nm fimbrial shaft. The lengths of the tip fibrillae vary (see insets for two examples), but they are normally much longer on P fimbriae than on type 1 fimbriae. Magnifications: ×60,000 (A) and ×200,000 (B and C) (see also Fig. 4.20 ).

Citation: Ofek I, Hasty D, Doyle R. 2003. Adhesins as Bacterial Cell Surface Structures: General Concepts of Structure, Biogenesis, and Regulation, p 63-96. In Bacterial Adhesion to Animal Cells and Tissues. ASM Press, Washington, DC. doi: 10.1128/9781555817800.ch4
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Image of FIGURE 4.15
FIGURE 4.15

Electron micrographs of a negatively stained strain expressing 987P fimbriae. These fimbriae are also peritrichously arranged (A), but at high magnification their architecture is such that they are thinner and much more flexible than P or type 1 fimbriae (B). The strain was provided by Robert Edwards and Dieter Schifferli. Magnifications, ×19,125 (A) and ×25,500 (B).

Citation: Ofek I, Hasty D, Doyle R. 2003. Adhesins as Bacterial Cell Surface Structures: General Concepts of Structure, Biogenesis, and Regulation, p 63-96. In Bacterial Adhesion to Animal Cells and Tissues. ASM Press, Washington, DC. doi: 10.1128/9781555817800.ch4
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Image of FIGURE 4.16
FIGURE 4.16

Electron micrographs of a negatively stained serovar Typhimurium strain expressing curli. These adhesins are long, thin, and much more flexible than even 987P fimbriae. (A) When cells are grown at 26°C, they produce a thick mat of curli surrounding the cell. (B) At higher magnification, individual filaments can be seen more easily. Magnifications, ×33,000 (A) and 75,000 (B).

Citation: Ofek I, Hasty D, Doyle R. 2003. Adhesins as Bacterial Cell Surface Structures: General Concepts of Structure, Biogenesis, and Regulation, p 63-96. In Bacterial Adhesion to Animal Cells and Tissues. ASM Press, Washington, DC. doi: 10.1128/9781555817800.ch4
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Image of FIGURE 4.17
FIGURE 4.17

Electron micrograph of a negatively stained strain expressing type IV fimbriae. Type IV fimbriae are straight and rigid in appearance but form into large, easily identified bundles. In electron micrographs of these bundles are typically seen broken off and separated from the cells, possibly due to the extreme forces applied to the large structures by surface tension of the medium or buffer as it dries during preparation of the electron microscope grid. Magnification, ×20,700.

Citation: Ofek I, Hasty D, Doyle R. 2003. Adhesins as Bacterial Cell Surface Structures: General Concepts of Structure, Biogenesis, and Regulation, p 63-96. In Bacterial Adhesion to Animal Cells and Tissues. ASM Press, Washington, DC. doi: 10.1128/9781555817800.ch4
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Image of FIGURE 4.18
FIGURE 4.18

Schematic illustration of the locus for P-pilus expression and the mechanism of regulation. As indicated, and encode regulatory elements, encodes the major subunit (see Fig. 4.14 ), encodes the usher, encodes the periplasmic chaperone, and encode components of the tip fibrillum, and encodes the Gal(α1→4)Gal binding tip adhesin. Expression of fimbrial genes is regulated by methylation of proximal (GATC) or distal (GATC) nucleotide sequences in the region between the divergently transcribed and genes. This affects the binding of Lrp and hence gene expression, as described in the text and references cited.

Citation: Ofek I, Hasty D, Doyle R. 2003. Adhesins as Bacterial Cell Surface Structures: General Concepts of Structure, Biogenesis, and Regulation, p 63-96. In Bacterial Adhesion to Animal Cells and Tissues. ASM Press, Washington, DC. doi: 10.1128/9781555817800.ch4
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Image of FIGURE 4.19
FIGURE 4.19

Schematic illustration of the locus for type 1 fimbria expression and the mechanism of regulation. As indicated, and encode regulatory elements, encodes the major subunit, encodes the periplasmic chaperone, encodes the outer membrane usher, and encode components of the tip fibrillum, and encodes the mannose binding tip adhesin. Expression of fimbrial genes is regulated by the inversion of a DNA segment located between and and containing the promoter. In the “on” orientation, is successfully transcribed. In the “off” orientation, the transcript is aborted, as described in the text and references cited.

Citation: Ofek I, Hasty D, Doyle R. 2003. Adhesins as Bacterial Cell Surface Structures: General Concepts of Structure, Biogenesis, and Regulation, p 63-96. In Bacterial Adhesion to Animal Cells and Tissues. ASM Press, Washington, DC. doi: 10.1128/9781555817800.ch4
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Image of FIGURE 4.20
FIGURE 4.20

Schematic illustration of fimbrial biogenesis. The mechanisms are remarkably similar for type P and 1 fimbriae, the best-studied examples of fimbrial biogenesis. Nascent polypeptides of fimbrial subunits are transported across the inner membrane by the general secretion (type II) pathway. The periplasmic chaperone binds to the polypeptide as it is being transported, and the chaperone aids in folding the subunits into a polymerization-competent conformation. The chaperone-subunit complexes arrive at the outer membrane usher, where they bind to previously delivered subunits, traverse the outer membrane as a ~2- nm-diameter linear filament, and then coil into a helical form at the external face of the usher. In this pathway, the translocation of subunits is highly ordered, with translocation of tip adhesin being followed by that of other tip fibrillum subunits and, finally, the major subunit protein.

Citation: Ofek I, Hasty D, Doyle R. 2003. Adhesins as Bacterial Cell Surface Structures: General Concepts of Structure, Biogenesis, and Regulation, p 63-96. In Bacterial Adhesion to Animal Cells and Tissues. ASM Press, Washington, DC. doi: 10.1128/9781555817800.ch4
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Image of FIGURE 4.21
FIGURE 4.21

Electron micrographs of rotary shadowed, purified type 1 fimbriae. (A) Purified type 1 fimbriae bound to mica in water. (B) Purified type 1 fimbriae bound to mica after a brief incubation in a 50% glycerol solution. Glycerol does not dissociate subunits into monomers but instead unravels the fimbrial helix. This image illustrates an early stage in the unraveling process, but eventually the 7-nm helical structure is converted into filaments of roughly 2 nm. Magnification, ×49,500.

Citation: Ofek I, Hasty D, Doyle R. 2003. Adhesins as Bacterial Cell Surface Structures: General Concepts of Structure, Biogenesis, and Regulation, p 63-96. In Bacterial Adhesion to Animal Cells and Tissues. ASM Press, Washington, DC. doi: 10.1128/9781555817800.ch4
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References

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Tables

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TABLE 4.1

Mechanisms for anchoring adhesins on bacterial cell surfaces

Citation: Ofek I, Hasty D, Doyle R. 2003. Adhesins as Bacterial Cell Surface Structures: General Concepts of Structure, Biogenesis, and Regulation, p 63-96. In Bacterial Adhesion to Animal Cells and Tissues. ASM Press, Washington, DC. doi: 10.1128/9781555817800.ch4
Generic image for table
TABLE 4.2

Examples of gram-positive proteins covalently anchored to cell walls

Citation: Ofek I, Hasty D, Doyle R. 2003. Adhesins as Bacterial Cell Surface Structures: General Concepts of Structure, Biogenesis, and Regulation, p 63-96. In Bacterial Adhesion to Animal Cells and Tissues. ASM Press, Washington, DC. doi: 10.1128/9781555817800.ch4
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TABLE 4.3

Examples of regulation of expression of adhesins in gram-positive bacteria

Citation: Ofek I, Hasty D, Doyle R. 2003. Adhesins as Bacterial Cell Surface Structures: General Concepts of Structure, Biogenesis, and Regulation, p 63-96. In Bacterial Adhesion to Animal Cells and Tissues. ASM Press, Washington, DC. doi: 10.1128/9781555817800.ch4
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TABLE 4.4

Mechanisms of biogenesis of gram-negative fimbriae

Citation: Ofek I, Hasty D, Doyle R. 2003. Adhesins as Bacterial Cell Surface Structures: General Concepts of Structure, Biogenesis, and Regulation, p 63-96. In Bacterial Adhesion to Animal Cells and Tissues. ASM Press, Washington, DC. doi: 10.1128/9781555817800.ch4
Generic image for table
TABLE 4.5

Examples of phase variation of gram-negative fimbria expression

Citation: Ofek I, Hasty D, Doyle R. 2003. Adhesins as Bacterial Cell Surface Structures: General Concepts of Structure, Biogenesis, and Regulation, p 63-96. In Bacterial Adhesion to Animal Cells and Tissues. ASM Press, Washington, DC. doi: 10.1128/9781555817800.ch4

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