Improvement of human interferon alpha secretion by Lactococcus lactis

Zhang, Qiuxiang; Zhong, Jin; Liang, Xiaobo; Chen, Li; Huan, Liandong

doi:10.1007/s10529-010-0285-x

Cited by 18 publications

(14 citation statements)

References 17 publications

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“…In some lactobacilli, up to 10-15 % of the total proteins are S-layer proteins, indicating high production and efficient secretion of these proteins. Since S-layer proteins are produced in high amounts, the cognate promoters and/or signal peptides have been exploited for expression and secretion of heterologous proteins in LAB [73][74][75][76][77]. S-layer proteins contain a region that binds strongly to the cell envelope.…”

Section: Non-covalent Binding-domain-mediated Anchoringmentioning

confidence: 99%

Display of recombinant proteins at the surface of lactic acid bacteria: strategies and applications

et al. 2016

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Lactic acid bacteria (LAB) are promising vectors of choice to deliver active molecules to mucosal tissues. They are recognized as safe by the World Health Organization and some strains have probiotic properties. The wide range of potential applications of LAB-driven mucosal delivery includes control of inflammatory bowel disease, vaccine delivery, and management of auto-immune diseases. Because of this potential, strategies for the display of proteins at the surface of LAB are gaining interest. To display a protein at the surface of LAB, a signal peptide and an anchor domain are necessary. The recombinant protein can be attached to the membrane layer, using a transmembrane anchor or a lipoprotein-anchor, or to the cell wall, by a covalent link using sortase mediated anchoring via the LPXTG motif, or by non-covalent liaisons employing binding domains such as LysM or WxL. Both the stability and functionality of the displayed proteins will be affected by the kind of anchor used. The most commonly surfaced exposed recombinant proteins produced in LAB are antigens and antibodies and the most commonly used LAB are lactococci and lactobacilli. Although it is not necessarily so that surface-display is the preferred localization in all cases, it has been shown that for certain applications, such as delivery of the human papillomavirus E7 antigen, surface-display elicits better biological responses, compared to cytosolic expression or secretion. Recent developments include the display of peptides and proteins targeting host cell receptors, for the purpose of enhancing the interactions between LAB and host. Surface-display technologies have other potential applications, such as degradation of biomass, which is of importance for some potential industrial applications of LAB.

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Section: Non-covalent Binding-domain-mediated Anchoringmentioning

confidence: 99%

Display of recombinant proteins at the surface of lactic acid bacteria: strategies and applications

et al. 2016

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“…The expression and/or secretion signals of Lactobacillus S-layer protein genes have also been utilized in biotechnological applications (Savijoki et al 1997; Kahala and Palva 1999; Novotny et al 2005; Lizier et al 2010; Zhang et al 2010a). The region encompassing the double promoter and the ribosome-binding sequence up to the start of the slpA gene of L. brevis ATCC 8287 (Kahala and Palva 1999), or the region containing additionally the slpA signal peptide gene sequence (Savijoki et al 1997), have been used in Lactobacillus and Lactococcus hosts for intracellular or extracellular protein production.…”

Section: Applications Of Lactobacillus S-layer Proteinsmentioning

confidence: 99%

“…The transcriptional activity in heterologous hosts could be significantly improved or decreased by the modification of native slp gene promoter, and both strain- and context-dependent effects of the introduced sequences have been detected (McCracken and Timms 1999). Adding merely the signal peptide encoding sequence of slpA from L. brevis ATCC 8287 upstream of the 5′ end of the human interferon alpha gene increased the secretion efficiency of interferon alpha in L. lactis threefold compared to the signal peptide encoding sequence of lactococcal Usp45, but the total interferon production was lower in the strain with the slpA signal peptide encoding sequence (Zhang et al 2010a). The recent development of a counterselective gene replacement system for the chromosomal integration of genes in L. acidophilus (Goh et al 2009) has enabled protein production using chromosomally located S-layer protein promoters in lactobacilli.…”

Section: Applications Of Lactobacillus S-layer Proteinsmentioning

confidence: 99%

Lactobacillus surface layer proteins: structure, function and applications

Hynönen

Palva

2013

Appl Microbiol Biotechnol

221

196

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Bacterial surface (S) layers are the outermost proteinaceous cell envelope structures found on members of nearly all taxonomic groups of bacteria and Archaea. They are composed of numerous identical subunits forming a symmetric, porous, lattice-like layer that completely covers the cell surface. The subunits are held together and attached to cell wall carbohydrates by non-covalent interactions, and they spontaneously reassemble in vitro by an entropy-driven process. Due to the low amino acid sequence similarity among S-layer proteins in general, verification of the presence of an S-layer on the bacterial cell surface usually requires electron microscopy. In lactobacilli, S-layer proteins have been detected on many but not all species. Lactobacillus S-layer proteins differ from those of other bacteria in their smaller size and high predicted pI. The positive charge in Lactobacillus S-layer proteins is concentrated in the more conserved cell wall binding domain, which can be either N- or C-terminal depending on the species. The more variable domain is responsible for the self-assembly of the monomers to a periodic structure. The biological functions of Lactobacillus S-layer proteins are poorly understood, but in some species S-layer proteins mediate bacterial adherence to host cells or extracellular matrix proteins or have protective or enzymatic functions. Lactobacillus S-layer proteins show potential for use as antigen carriers in live oral vaccine design because of their adhesive and immunomodulatory properties and the general non-pathogenicity of the species.

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“…In addition, in L. lactis, the nine-residue synthetic propeptide, LEISSTCDA, which is fused immediately after the signal peptide cleavage site, is known to enhance heterologous protein secretion (Le Loir et al, 1998;Le Loir et al, 2005;Zhuang et al, 2008;Zhang et al, 2010). Therefore, we evaluated whether the fusion of the AmyE signal peptide and the propeptide could improve the secretion of hIFNα-2b, compared to that with only AmyE signal peptide.…”

Section: Propeptidementioning

confidence: 99%