Assembly of pili on the surface of <i>Bacillus cereus</i> vegetative cells

Budzik, Jonathan M.; Marraffini, Luciano A.; Schneewind, Olaf

doi:10.1111/j.1365-2958.2007.05939.x

Cited by 93 publications

(133 citation statements)

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“…Plasmids-The following plasmids contain B. cereus pilus genes cloned under control of the spac promoter of pLM5 (12) and were described previously: pJB39 (bcpA-srtD), pJB12 (bcpA-srtD-bcpB), pJB28 (bcpA K162A -srtD-bcpB), pJB32 (bcpAsrtD C207A -bcpB), and pJB48 (bcpA LAVAA -srtD-bcpB) (15). pJB182 encodes for bcpA-srtD-bcpB ⌬VIPNTGG719 , which contains a seven-residue deletion in BcpB, encompassing the IPNTG sorting signal motif and one residue flanking each end (VIPNTGG 719 ).…”

Section: Methodsmentioning

confidence: 99%

“…After translocation across the plasma membrane, P2 precursor species arise from removal of the signal peptide from P1 precursors by a signal peptidase (16). Bacillus cereus pili are composed of two subunits; that is, the major pilin, BcpA, and the minor pilin, BcpB (15). In contrast to BcpA, which is deposited throughout the pilus, BcpB is found at fiber tip (15).…”

mentioning

confidence: 99%

“…However, the molecular mechanism whereby bacilli deposit BcpB, the minor pilin, at the tip of BcpA pili is not known. Although the BcpB precursor harbors an N-terminal signal peptide and a C-terminal IPNTG sorting signal, it lacks the YPKN pilin motif of the major subunit (15). Furthermore, the substrate properties of the BcpB IPNTG sorting signal for the four classes of sortases expressed by bacilli has yet to be established.…”

mentioning

confidence: 99%

“…Bacillus cereus pili are composed of two subunits; that is, the major pilin, BcpA, and the minor pilin, BcpB (15). In contrast to BcpA, which is deposited throughout the pilus, BcpB is found at fiber tip (15). Sortase D cleaves the BcpA LPXTG motif sorting signal between the threonine and glycine residues to form an amide bond to the ⑀-amino group of the lysine within the YPKN motif of adjacent BcpA subunits (16).…”

mentioning

confidence: 99%

“…Sortase C cuts LPNTA sorting signals and anchors proteins to the peptidoglycan cross-bridges in sporulating bacteria (12,13). Finally, sortase D catalyzes transpeptidation reactions in the assembly of pili (14,15). Sortase D recognizes the amino group of lysine residues within the YPKN motif of pilin subunits as nucleophiles (16).…”

mentioning

confidence: 99%

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Sortase D Forms the Covalent Bond That Links BcpB to the Tip of Bacillus cereus Pili

Budzik¹,

Schneewind

2009

Journal of Biological Chemistry

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Section: Methodsmentioning

confidence: 99%

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Sortase D Forms the Covalent Bond That Links BcpB to the Tip of Bacillus cereus Pili

Budzik¹,

Schneewind

2009

Journal of Biological Chemistry

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Bacterial Pili and Fimbriae

Huang

Dwivedi

Ton‐That

2010

Encyclopedia of Life Sciences

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Bacterial proteinaceous filaments termed pili or fimbriae are nonflagellar, hair‐like structures protruding from the cell surface that are critical for bacterial virulence and fitness. Present in both Gram‐negative and Gram‐positive bacteria, pili are involved in many processes such as conjugation, adherence, twitching motility, biofilm formation and immunomodulation. Considerably diverse and complex, Gram‐negative pili are formed by noncovalent polymerisation of various pilin subunits; many of these pili require chaperones and usher proteins for their assembly. In contrast, fewer pilus systems have been described for the Gram‐positive counterparts; notably well studied are the heterotrimeric or ‐dimeric pili that are covalently assembled by a transpeptidase enzyme called sortase . Here we review the current knowledge of assembly pathways, structure and function of these pili in Gram‐negative and Gram‐positive pathogens. Key Concepts: Noncovalent pilus polymerisation is a general mechanism of pilus assembly in Gram‐negative bacteria, including the chaperon‐usher assembly pathway and type IV pilus pathway, which generates noncovalent pilus polymers. Sortase‐mediated pilus assembly is a general mechanism of pilus assembly in Gram‐positive bacteria that involves a transpeptidase enzyme named sortase, which cleaves pilin precursors at sorting signals between threonine and glycine and involve the side‐chain amino groups of pilin motif sequences to generate covalent links between pilin subunits. The sorting signal is consisted of an LPXTG motif followed by a hydrophobic domain and a positively charged tail. The pilin motif is an 11 amino acid sequence of WxxxVxVYPKN located near the N ‐terminus of major pilin subunits, in which the electron donating lysine residue forms an isopeptide bond with the threonine residue generated from the cleavage of the LPXTG motif of adjacent pilin subunits. Tissue tropism is referred to as the ability of a pathogen to adhere specifically to some particular epithelial cells. Phase variation involves switching of surface antigens such as pili that allows a pathogen to evade the host immune system. Immunomodulation is a process of changing the host's immune system by certain molecules known as immunomodulators including pili that can activate or suppress immune cells. Dental plaque is one of the most complex bacterial biofilms that is formed by sequential colonisation of initial colonisers such as Actinomyces spp. and oral streptococci and late colonisers; this process involves Actinomyces fimbriae. Twitching motility mediated by pili allows translocation between mucosal surfaces, colonisation of host tissues and establishment of biofilms by a pathogen.

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Bacterial Pili and Fimbriae

Ramirez

Ton‐That

2020

Encyclopedia of Life Sciences

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Bacterial proteinaceous filaments termed pili or fimbriae are nonflagellar, hair‐like structures protruding from the cell surface that are critical for bacterial virulence and fitness. Present in both Gram‐negative and Gram‐positive bacteria, pili are involved in many processes such as conjugation, adherence, twitching motility, biofilm formation and immunomodulation. Considerably diverse and complex, Gram‐negative pili are formed by noncovalent polymerisation of various pilin subunits; many of these pili require chaperones and usher proteins for their assembly. In contrast, fewer pilus systems have been described for the Gram‐positive counterparts; notably well studied are the heterotrimeric or ‐dimeric pili that are covalently assembled by a transpeptidase enzyme called sortase. Furthermore, type IV pili have been identified in several Gram‐positive bacteria, especially in clostridia. Key Concepts Noncovalent pilus polymerisation is a general mechanism of pilus assembly in Gram‐negative bacteria, including the chaperone/usher assembly pathway and type IV pilus pathway, which generates noncovalent pilus polymers. Sortase‐mediated pilus assembly is a general mechanism of pilus assembly in Gram‐positive bacteria that involves a transpeptidase enzyme named sortase, which cleaves pilin precursors at sorting signals between threonine and glycine residues and utilises the side‐chain amino groups of pilin motif sequences to generate covalent links between pilin subunits. The sorting signal consists of an LPXTG motif followed by a hydrophobic domain and a positively charged tail. The pilin motif is an 11 amino acid sequence of WxxxVxVYPKN located near the N ‐terminus of major pilin subunits, in which the electron‐donating lysine residue forms an isopeptide bond with the threonine residue generated from the cleavage of the LPXTG motif of adjacent pilin subunits. Tissue tropism is referred to as the ability of a pathogen to adhere specifically to some particular epithelial cells. Phase variation involves switching of surface antigens such as pili that allows a pathogen to evade the host immune system. Immunomodulation is a process of changing the host's immune system by certain molecules known as immunomodulators including pili that can activate or suppress immune cells. Dental plaque is one of the most complex bacterial biofilms that is formed by sequential colonisation of initial colonisers such as Actinomyces spp. and oral streptococci and late colonisers; this process involves Actinomyces fimbriae. Twitching motility mediated by pili allows translocation between mucosal surfaces, colonisation of host tissues and establishment of biofilms by a pathogen.

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Assembly of pili on the surface of Bacillus cereus vegetative cells

Cited by 93 publications

References 70 publications

Sortase D Forms the Covalent Bond That Links BcpB to the Tip of Bacillus cereus Pili

Sortase D Forms the Covalent Bond That Links BcpB to the Tip of Bacillus cereus Pili

Bacterial Pili and Fimbriae

Bacterial Pili and Fimbriae

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