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5 Bacterial Adherence to Cell Surfaces and Extracellular Matrix

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5 Bacterial Adherence to Cell Surfaces and Extracellular Matrix, Page 1 of 2

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Abstract:

An essential step in the successful colonization and production of disease by microbial pathogens is their ability to adhere to host cell surfaces and the underlying extracellular matrix. The choice of host cell substrate that a pathogen can adhere to is large. The mammalian cell surface contains many proteins, glycoproteins, glycolipids, and other carbohydrates that could potentially serve as a receptor for an adhesin. Additionally, the extracellular matrix provides a rich source of glycoproteins for adhesins to bind to and even initiate signaling, and implanted devices remain a major target for bacterial adherence. , the causative agent of whooping cough, is a respiratory mucosal pathogen that possesses several potential adherence factors that exemplify the complexity of bacterial adherence to host cell surfaces. and are two mucosal pathogens that have developed sophisticated and overlapping mechanisms to adhere to host cell surfaces. Two high-molecular-weight adhesins (HMW1 and HMW2) belong to the autotransporter family and mediate bacterial adherence. Adhesins play an important role in disease and represent the interface between the pathogen and the host cell. In many cases the precise role that individual adhesins play in the pathogenesis of specific diseases has been established. For example, inactivation of the gene which encodes Cna, a collagen-binding adhesin of , results in a mutant with a considerably diminished capacity to cause septic arthritis in an animal model.

Citation: Finlay B, Caparon M. 2004. 5 Bacterial Adherence to Cell Surfaces and Extracellular Matrix, p 105-120. In Cossart P, Boquet P, Normark S, Rappuoli R (ed), Cellular Microbiology, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555817633.ch5

Key Concept Ranking

Type III Secretion System
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Type II Secretion System
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Type III Secretion System
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Type II Secretion System
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Outer Membrane Proteins
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Figures

Image of Figure 5.1
Figure 5.1

Bacterial adherence to host cell surfaces. Bacteria can adhere to host cell surfaces either directly by using a surface-anchored adhesin or indirectly by binding a soluble host component that then serves as a bridge between the bacterial adhesin and the natural host receptor for that molecule.

Citation: Finlay B, Caparon M. 2004. 5 Bacterial Adherence to Cell Surfaces and Extracellular Matrix, p 105-120. In Cossart P, Boquet P, Normark S, Rappuoli R (ed), Cellular Microbiology, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555817633.ch5
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Image of Figure 5.2
Figure 5.2

Schematic of P pilus operon and biogenesis. (Adapted from 887–901, 1993.)

Citation: Finlay B, Caparon M. 2004. 5 Bacterial Adherence to Cell Surfaces and Extracellular Matrix, p 105-120. In Cossart P, Boquet P, Normark S, Rappuoli R (ed), Cellular Microbiology, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555817633.ch5
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Image of Figure 5.3
Figure 5.3

Schematic of various gram-negative adhesins.

Citation: Finlay B, Caparon M. 2004. 5 Bacterial Adherence to Cell Surfaces and Extracellular Matrix, p 105-120. In Cossart P, Boquet P, Normark S, Rappuoli R (ed), Cellular Microbiology, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555817633.ch5
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Image of Figure 5.4
Figure 5.4

Domain architecture of protein F. Protein F is a member of a large family of related surface proteins found among the gram-positive cocci that bind to fibronectin. The signature feature of this family is a repetitive domain consisting of 32 to 44 amino acids that is repeated two to six times in tandem. This domain consists of 37 amino acids in protein F and is known as RD2. Sequences highly conserved in the repetitive region from different relatives of protein F are highlighted in bold type. This repetitive domain binds to the amino-terminal 29-kDa fibrin-binding domain of fibronectin, and the minimal functional binding domain of RD2 includes 44 amino acid residues derived from the carboxy-terminal segment of one repeat and the amino-terminal segment of the adjacent repeat, as is shown underneath RD2. This binding unit begins and terminates with amino acid motif MGGQSES (underlined). Other common features include a signal sequence (S), a long amino-terminal nonrepetitive region of sequence that is unique to different family members (U), and a second repetitive region of unknown function (called RD1 in protein F). The proteins also share features common to many surface proteins of gram-positive cocci, including a proline- and lysine-rich domain that may interact with the cell wall (W), a hydrophobic domain that may interact with the membrane (M), a short tail of charged amino acids (C), and an LPXTG motif (LPATG in protein F) that serves as a processing site, in which the protein becomes cleaved after the threonine and is cross-linked to a lysine residue of the peptidoglycan cell wall. Some members of this family contain an additional domain for binding to fibronectin which can be located in various regions amino terminal to the repetitive domain. In protein F, this domain is known as UR, and it is composed of 43 amino acids immediately N terminal to RD2, as is shown above UR. The ability of UR to bind to fibronectin also has an absolute requirement for the first six amino acids from the first repeat unit of RD2. UR binds to a region of fibronectin that includes the amino-terminal 29-kDa domain and the adjacent 40-kDa collagen-binding domains. The various domains are not shown to scale.

Citation: Finlay B, Caparon M. 2004. 5 Bacterial Adherence to Cell Surfaces and Extracellular Matrix, p 105-120. In Cossart P, Boquet P, Normark S, Rappuoli R (ed), Cellular Microbiology, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555817633.ch5
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References

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1. Baumler, A. J.,, R. M. Tsolis,, P. J. Valentine,, T. A. Ficht,, and F. Heffron. 1997. Synergistic effect of mutations in invA and lpfC on the ability of Salmonella typhimurium to cause murine typhoid. Infect. Immun. 65:22542259. An interesting manuscript that begins to probe the complexity of adhesions on disease. Several more studies have shown that Salmonella has many adhesions and their roles are complex.
2. Evans, D. J., Jr.,, and D. G. Evans. 2000. Helicobacter pylori adhesins: review and perspectives. Helicobacter 5:183195.
3. Finlay, B. B.,, and S. Falkow. 1997. Common themes in microbial pathogenicity. II. Mol. Biol. Microbiol. Rev. 61:136169. A good overview of mechanisms of bacterial pathogenicity.
4. Hanski, E.,, and M. G. Caparon. 1992. Protein F, a fibronectin-binding protein, is an adhesin of the group A streptococcus, Streptococcus pyogenes. Proc. Natl. Acad. Sci. USA 89:61726176. Identification and characterization of protein F and its binding substrate.
5. Hauck, C. R. 2002. Cell adhesion receptors: signaling capacity and exploitation by bacterial pathogens. Med. Microbiol. Immunol. (Berlin) 191:5562.
6. Hauck, C. R.,, and T. F. Meyer. 2003. ‘Small’ talk: Opa proteins as mediators of Neisseria-host-cell communication. Curr. Opin. Microbiol. 6:4349.
7. Hultgren, S. J.,, S. Abraham,, M. Caparon,, P. Falk,, J. St. Geme, and S. Normark. 1993. Pilus and nonpilus bacterial adhesins: assembly and function in cell recognition. Cell 73:887901. A strong overview of bacterial adhesion mechanisms.
8. Kenny, B.,, R. DeVinney,, M. Stein,, D. J. Reinscheid,, E. A. Frey,, and B. B. Finlay. 1997. Enteropathogenic E. coli (EPEC) transfers its receptor for intimate adherence into mammalian cells. Cell 91:511520.
9. Langermann, S.,, S. Palaszynski,, M. Barnhart,, G. Auguste,, J. S. Pinkner,, J. H. Burlein,, P. Barren,, S. Koenig,, S. Leath,, C. H. Jones,, and S. J. Hultgren. 1997. Prevention of mucosal Escherichia coli infection by FimH-adhesin-based systemic vaccination. Science 276:607611. Proof of concept that adhesins can be blocked by vaccination.
10. Menozzi, F. D.,, K. Pethe,, P. Bifani,, F. Soncin,, M. J. Brennan,, and C. Locht. 2002. Enhanced bacterial virulence through exploitation of host glycosaminoglycans. Mol. Microbiol. 43:13791386.
11. Nougayrede, J. P.,, P. J. Fernandes,, and M. S. Donnenberg. 2003. Adhesion of enteropathogenic Escherichia coli to host cells. Cell Microbiol. 5:359372.
12. Ozeri, V.,, A. Tovi,, I. Burstein,, S. Natanson-Yaron,, M. G. Caparon,, K. M. Yamada,, S. K. Akiyama,, I. Vlodavsky,, and E. Hanski. 1996. A two-domain mechanism for group A streptococcal adherence through protein F to the extracellular matrix. EMBO J. 15:898998.
13. Patti, J. M.,, B. L. Allen,, M. J. McGavin,, and M. Höök. 1994. MSCRAMM-mediated adherence of microoganisms to host tissues. Annu. Rev. Microbiol. 48:585617.
14. Patti, J., M, T. Bremell,, D. Krajewska-Pietrasik,, A. Abdelnour,, A. Tarkowski,, C. Ryden,, and M. Höök. 1994. The Staphylococcus aureus collagen adhesin is a virulence determinant in experimental septic arthritis. Infect. Immun. 62:152161.
15. Pepe, J. C.,, M. R. Wachtel,, E. Wagar,, and V. L. Miller. 1995. Pathogenesis of defined invasion mutants of Yersinia enterocolitica in a BALB/c mouse model of infection. Infect. Immun. 63:48374848. An interesting report of the complexity of adhesins and invasins and their contribution to disease.
16. Rambukkana, A.,, J. L. Salzer,, P. D. Yurchenco,, and E. I. Tuomanen. 1997. Neural targeting of Mycobacterium leprae mediated by the G domain of the laminin-alpha2 chain. Cell 88:811821.
17. St. Geme, J. W., III. 2002. Molecular and cellular determinants of non-typeable Haemophilus influenzae adherence and invasion. Cell Microbiol. 4:191200.

Tables

Generic image for table
Table 5.1

Selected examples of the interactions between some gram-positive bacteria and various components of the extracellular matrix

Citation: Finlay B, Caparon M. 2004. 5 Bacterial Adherence to Cell Surfaces and Extracellular Matrix, p 105-120. In Cossart P, Boquet P, Normark S, Rappuoli R (ed), Cellular Microbiology, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555817633.ch5

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