Structure-Function Analysis of Immunity Proteins of Pediocin-Like Bacteriocins: C-Terminal Parts of Immunity Proteins Are Involved in Specific Recognition of Cognate Bacteriocins

Johnsen, Line; Fimland, Gunnar; Mantzilas, Dimitris; Nissen‐Meyer, Jon

doi:10.1128/aem.70.5.2647-2652.2004

Cited by 30 publications

(52 citation statements)

References 38 publications

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“…Later, the structure of subgroup B immunity protein (piscicolin 126-im) was shown to have the conserved fourhelix bundle but relatively shorter and less flexible C-terminal part (Martin-Visscher et al 2008). Structural studies on hybrid immunity proteins proposed that the C-terminal parts of the immunity proteins determine the immunity and specific recognition of the C-terminal hairpin of class IIa bacteriocins (Johnsen et al 2004;Johnsen et al 2005a). Moreover, piscicolin 126 immunity protein contains a C-terminal hydrophobic pocket comprising residues that are highly conserved in subgroup B immunity proteins (Martin-Visscher et al…”

Section: Bacteriocin Immunitymentioning

confidence: 99%

“…Besides, the function of immunity protein has been found to be strain-dependent (Johnsen et al 2005a). Therefore, instead of direct binding to the bacteriocins, the immunity proteins may interact with a receptor protein which varies in different strains (Figure 2 and Figure 3, p30) (Fimland et al 2002a;Johnsen et al 2004). …”

Section: ) As Hydrophobic Interactions Are Normally Involved In mentioning

confidence: 99%

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Genetic characterisation and heterologous expression of leucocin C, a class IIa bacteriocin from Leuconostoc carnosum 4010

Wan

Saris

et al. 2012

Appl Microbiol Biotechnol

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Section: Bacteriocin Immunitymentioning

confidence: 99%

Section: ) As Hydrophobic Interactions Are Normally Involved In mentioning

confidence: 99%

Genetic characterisation and heterologous expression of leucocin C, a class IIa bacteriocin from Leuconostoc carnosum 4010

Wan

Saris

et al. 2012

Appl Microbiol Biotechnol

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“…The immunity proteins show a high degree of specificity with respect to the bacteriocin they recognize, although some immunity proteins render cells immune to a few pediocin-like bacteriocins in addition to their cognate bacteriocin (22). Using hybrid immunity proteins and hybrid bacteriocins, it was recently shown that the C-terminal half of the immunity proteins contains a region that is involved in specific recognition of the C-terminal hairpin-like domain of the bacteriocin they confer immunity to (15,23). The mode of action of the immunity proteins is not known, but their effectiveness is strain-dependent, and the functionality of the immunity proteins thus appears to depend partly on strain-dependent factors (22,23).…”

mentioning

confidence: 99%

“…The branes; exposing the proteins to lipid micelles does not induce gross alterations in the protein conformation (23). The threedimensional structure of the pediocin-like immunity protein for carnobacteriocin B2 has recently been determined by NMR spectroscopy (26).…”

mentioning

confidence: 99%

“…Using hybrid immunity proteins and hybrid bacteriocins, it was recently shown that the C-terminal half of the immunity proteins contains a region that is involved in specific recognition of the C-terminal hairpin-like domain of the bacteriocin they confer immunity to (15,23). The mode of action of the immunity proteins is not known, but their effectiveness is strain-dependent, and the functionality of the immunity proteins thus appears to depend partly on strain-dependent factors (22,23). It has been suggested that they may act by disturbing the interaction between the bacteriocin and a (putative) membrane-located bacteriocin receptor (19,24,25).…”

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confidence: 99%

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1.6-Å Crystal Structure of EntA-im

Johnsen

Dalhus

Leiros

et al. 2005

Journal of Biological Chemistry

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Many Gram-positive bacteria produce ribosomally synthesized antimicrobial peptides, often termed bacteriocins. Genes encoding pediocin-like bacteriocins are generally cotranscribed with or in close vicinity to a gene encoding a cognate immunity protein that protects the bacteriocin-producer from their own bacteriocin. We present the first crystal structure of a pediocin-like immunity protein, EntA-im, conferring immunity to the bacteriocin enterocin A. Determination of the structure of this 103-amino acid protein revealed that it folds into an antiparallel four-helix bundle with a flexible C-terminal part. The fact that the immunity protein conferring immunity to carnobacteriocin B2 also consists of a four-helix bundle (Sprules, T., Kawulka, K. E., and Vederas, J. C. (2004) Biochemistry 43, 11740 -11749) strongly indicates that this is a conserved structural motif in all pediocinlike immunity proteins. The C-terminal half of the immunity protein contains a region that recognizes the C-terminal half of the cognate bacteriocin, and the flexibility in the C-terminal end of the immunity protein might thus be an important characteristic that enables the immunity protein to interact with its cognate bacteriocin. By homology modeling of three other pediocin-like immunity proteins and calculation of the surface charge distribution for EntA-im and the three structure models, different charge distributions were observed. The differences in the latter part of helix 3, the beginning of helix 4, and the loop connecting these helices might also be of importance in determining the specificity.

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Pediocin‐like antimicrobial peptides (class IIa bacteriocins) and their immunity proteins: biosynthesis, structure, and mode of action

Fimland

Johnsen

Dalhus

et al. 2005

Journal of Peptide Science

185

158

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Pediocin-like antimicrobial peptides (AMPs) form a group of lactic acid bacteria produced, cationic membrane-permeabilizing peptides with 37 to 48 residues. Upon exposure to membrane-mimicking entities, their hydrophilic, cationic, and highly conserved N-terminal region forms a three-stranded antiparallel beta-sheet supported by a conserved disulfide bridge. This N-terminal beta-sheet region is followed by a central amphiphilic alpha-helix and this in most (if not all) of these peptides is followed by a rather extended C-terminal tail that folds back onto the central alpha-helix, thereby creating a hairpin-like structure in the C-terminal half. There is a flexible hinge between the beta-sheet N-terminal region and the hairpin C-terminal region and one thus obtains two domains that may move relative to each other. The cationic N-terminal beta-sheet domain mediates binding of the pediocin-like AMPs to the target-cell surface through electrostatic interactions, while the more hydrophobic and amphiphilic C-terminal hairpin domain penetrates into the hydrophobic part of the target-cell membrane, thereby mediating leakage through the membrane. The hinge provides the structural flexibility that enables the C-terminal hairpin domain to dip into the hydrophobic part of the membrane. Despite extensive sequence similarities, these AMPs differ markedly in their target-cell specificity, and results obtained with hybrid AMPs indicate that the membrane-penetrating hairpin-like C-terminal domain is the major specificity determinant. Bacteria that produce pediocin-like AMPs also produce a 11-kDa cognate immunity protein that protects the producer. The immunity proteins are well-structured, 4-helix bundle cytosolic proteins. They show a high degree of specificity in that they largely recognize and confer immunity only to their cognate AMP and in some cases to a few AMPs that are closely related to their cognate AMP. The C-terminal half of the immunity proteins contains a domain that is involved in specific recognition of the C-terminal membrane-penetrating specificity-determining hairpin domain of the cognate AMP.

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Structure-Function Analysis of Immunity Proteins of Pediocin-Like Bacteriocins: C-Terminal Parts of Immunity Proteins Are Involved in Specific Recognition of Cognate Bacteriocins

Cited by 30 publications

References 38 publications

Genetic characterisation and heterologous expression of leucocin C, a class IIa bacteriocin from Leuconostoc carnosum 4010

Genetic characterisation and heterologous expression of leucocin C, a class IIa bacteriocin from Leuconostoc carnosum 4010

1.6-Å Crystal Structure of EntA-im

Pediocin‐like antimicrobial peptides (class IIa bacteriocins) and their immunity proteins: biosynthesis, structure, and mode of action

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