Pilus of : Structure, Function and Vaccine Potential

Overview

Journal Front Cell Infect Microbiol

Specialties Cell Biology
Infectious Diseases
Microbiology

Date 2023 Oct 6

PMID 37799336

Authors

Chenglin Miao

Yali Cui

Ziyi Yan

Yongmei Jiang

Affiliations

Soon will be listed here.

Abstract

The pilus is an extracellular structural part that can be detected in some () isolates (type I pili are found in approximately 30% of strains, while type II pili are found in approximately 20%). It is anchored to the cell wall by LPXTG-like motifs on the peptidoglycan. Two kinds of pili have been discovered, namely, pilus-1 and pilus-2. The former is encoded by pilus islet 1 (PI-1) and is a polymer formed by the protein subunits RrgA, RrgB and RrgC. The latter is encoded by pilus islet 2 (PI-2) and is a polymer composed mainly of the structural protein PitB. Although pili are not necessary for the survival of , they serve as the structural basis and as virulence factors that mediate the adhesion of bacteria to host cells and play a direct role in promoting the adhesion, colonization and pathogenesis of . In addition, as candidate antigens for protein vaccines, pili have promising potential for use in vaccines with combined immunization strategies. Given the current understanding of the pili of regarding the genes, proteins, structure, biological function and epidemiological relationship with serotypes, combined with the immunoprotective efficacy of pilins as protein candidates for vaccines, we here systematically describe the research status and prospects of pili and provide new ideas for subsequent vaccine research and development.

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References

Engholm D, Kilian M, Goodsell D, Andersen E, Kjaergaard R . A visual review of the human pathogen Streptococcus pneumoniae. FEMS Microbiol Rev. 2017; 41(6):854-879. DOI: 10.1093/femsre/fux037. View

Regev-Yochay G, Hanage W, Trzcinski K, Rifas-Shiman S, Lee G, Bessolo A . Re-emergence of the type 1 pilus among Streptococcus pneumoniae isolates in Massachusetts, USA. Vaccine. 2010; 28(30):4842-6. PMC: 2897942. DOI: 10.1016/j.vaccine.2010.04.042. View

Iovino F, Thorsdottir S, Henriques-Normark B . Receptor Blockade: A Novel Approach to Protect the Brain From Pneumococcal Invasion. J Infect Dis. 2018; 218(3):476-484. DOI: 10.1093/infdis/jiy193. View

Regev-Yochay G, Jaber H, Hamdan A, Daana M, Nammouz H, Thalji A . Vaccine escape of piliated Streptococcus pneumoniae strains. Vaccine. 2016; 34(25):2787-92. DOI: 10.1016/j.vaccine.2016.04.064. View

Kim G, Seon S, Rhee D . Pneumonia and Streptococcus pneumoniae vaccine. Arch Pharm Res. 2017; 40(8):885-893. PMC: 7090487. DOI: 10.1007/s12272-017-0933-y. View

Shaik M, Lombardi C, Trindade D, Fenel D, Schoehn G, Di Guilmi A . A structural snapshot of type II pilus formation in Streptococcus pneumoniae. J Biol Chem. 2015; 290(37):22581-92. PMC: 4566232. DOI: 10.1074/jbc.M115.647834. View

Kreikemeyer B, Gamez G, Margarit I, Giard J, Hammerschmidt S, Hartke A . Genomic organization, structure, regulation and pathogenic role of pilus constituents in major pathogenic Streptococci and Enterococci. Int J Med Microbiol. 2010; 301(3):240-51. DOI: 10.1016/j.ijmm.2010.09.003. View

Avci F . Novel strategies for development of next-generation glycoconjugate vaccines. Curr Top Med Chem. 2013; 13(20):2535-40. DOI: 10.2174/15680266113136660180. View

Gong X, Gao Y, Shu J, Zhang C, Zhao K . Chitosan-Based Nanomaterial as Immune Adjuvant and Delivery Carrier for Vaccines. Vaccines (Basel). 2022; 10(11). PMC: 9696061. DOI: 10.3390/vaccines10111906. View

10.

Figueira M, Moschioni M, De Angelis G, Barocchi M, Sabharwal V, Masignani V . Variation of pneumococcal Pilus-1 expression results in vaccine escape during Experimental Otitis Media [EOM]. PLoS One. 2014; 9(1):e83798. PMC: 3885439. DOI: 10.1371/journal.pone.0083798. View

11.

Moschioni M, de Angelis G, Melchiorre S, Masignani V, Leibovitz E, Barocchi M . Prevalence of pilus-encoding islets among acute otitis media Streptococcus pneumoniae isolates from Israel. Clin Microbiol Infect. 2009; 16(9):1501-4. DOI: 10.1111/j.1469-0691.2009.03105.x. View

12.

Iovino F, Engelen-Lee J, Brouwer M, van de Beek D, van der Ende A, Valls Seron M . pIgR and PECAM-1 bind to pneumococcal adhesins RrgA and PspC mediating bacterial brain invasion. J Exp Med. 2017; 214(6):1619-1630. PMC: 5461002. DOI: 10.1084/jem.20161668. View

13.

Zahner D, Gudlavalleti A, Stephens D . Increase in pilus islet 2-encoded pili among Streptococcus pneumoniae isolates, Atlanta, Georgia, USA. Emerg Infect Dis. 2010; 16(6):955-62. PMC: 3086225. DOI: 10.3201/eid1606.091820. View

14.

Narciso A, Iovino F, Thorsdottir S, Mellroth P, Codemo M, Spoerry C . Membrane particles evoke a serotype-independent cross-protection against pneumococcal infection that is dependent on the conserved lipoproteins MalX and PrsA. Proc Natl Acad Sci U S A. 2022; 119(23):e2122386119. PMC: 9191655. DOI: 10.1073/pnas.2122386119. View

15.

Bryce J, Boschi-Pinto C, Shibuya K, Black R . WHO estimates of the causes of death in children. Lancet. 2005; 365(9465):1147-52. DOI: 10.1016/S0140-6736(05)71877-8. View

16.

Naziga E, Wereszczynski J . Molecular Mechanisms of the Binding and Specificity of Streptococcus Pneumoniae Sortase C Enzymes for Pilin Subunits. Sci Rep. 2017; 7(1):13119. PMC: 5640630. DOI: 10.1038/s41598-017-13135-3. View

17.

Dramsi S, Trieu-Cuot P, Bierne H . Sorting sortases: a nomenclature proposal for the various sortases of Gram-positive bacteria. Res Microbiol. 2005; 156(3):289-97. DOI: 10.1016/j.resmic.2004.10.011. View

18.

Platt H, Omole T, Cardona J, Fraser N, Mularski R, Andrews C . Safety, tolerability, and immunogenicity of a 21-valent pneumococcal conjugate vaccine, V116, in healthy adults: phase 1/2, randomised, double-blind, active comparator-controlled, multicentre, US-based trial. Lancet Infect Dis. 2022; 23(2):233-246. DOI: 10.1016/S1473-3099(22)00526-6. View

19.

Ganaie F, Saad J, McGee L, van Tonder A, Bentley S, Lo S . A New Pneumococcal Capsule Type, 10D, is the 100th Serotype and Has a Large Fragment from an Oral Streptococcus. mBio. 2020; 11(3). PMC: 7240158. DOI: 10.1128/mBio.00937-20. View

20.

Kadioglu A, Weiser J, Paton J, Andrew P . The role of Streptococcus pneumoniae virulence factors in host respiratory colonization and disease. Nat Rev Microbiol. 2008; 6(4):288-301. DOI: 10.1038/nrmicro1871. View