Staphylococcal superantigen-like 12 activates murine bone marrow derived mast cells

Kobayashi, Masato; Kitano, Takuma; Nishiyama, Saishi; Sanjo, Hideki; Onozaki, Kikuo; Taki, Shinsuke; Itoh, Saotomo; Hida, Shigeaki

doi:10.1016/j.bbrc.2019.02.052

Cited by 11 publications

(11 citation statements)

References 23 publications

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“…We examined their abilities to induce the degranulation of BMMCs. SSL12N induced the release of a granule enzyme, β‐hexosaminidase from BMMCs at the concentration of 3.3 μg/ml or higher, as we reported previously (Kobayashi et al, 2019). On the other hand, SSL12M never induced the release of the enzyme at the concentration of 30 μg/ml (Figure 1b).…”

Section: Resultssupporting

confidence: 87%

“…S. aureus produces a broad range of toxins, and several toxins exhibit duplicate and complement functions. So far, δ‐toxin, PSM, α‐toxin, and SSL12 have been reported to affect mast cell function (Hayashi et al, 2019; Hodille et al, 2016; Kobayashi et al, 2019; Nakamura et al, 2013). A multi‐component vaccine that was comprised of plural toxins that activate mast cells should be developed for the prevention and treatment of allergic inflammation associated with S. aureus .…”

Section: Discussionmentioning

confidence: 99%

“…We previously reported that SSL12 activated two important immune cells in allergic inflammation; SSL12 induced the degranulation and the induction of IL-6 and IL-13 in murine bone marrow-derived mast cells (BMMCs) without cell damage (Kobayashi et al, 2019) and the production of IL-4 in murine bone marrow-derived basophils and murine fresh isolated basophils (Nishiyama et al, 2020). SSL12 would be one of the staphylococcal pathogenic factors in allergic inflammations.…”

Section: Introductionmentioning

confidence: 99%

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Identification of responsible amino acid residues in staphylococcal superantigen‐like 12 for the activation of mast cells

et al. 2022

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Staphylococcal superantigen‐like 12 (SSL12) is reported to evoke the degranulation in murine mast cells. The allelic variant of SSL12 in the genome of reference strain NCTC8325 induced the degranulation of murine mast cells, that of MRSA252 strain did not, nevertheless relatively high sequence similarity (82%). To identify responsible amino acid residues of SSL12 for mast cell activation, we created a series of domain swap mutants and amino acid substitution mutants between the active and inactive variants. The mutants that harbored oligonucleotide/oligosaccharide binding (OB)‐fold domain of the active variant activated mast cells. The replacement at position 56 (L56F) in the OB‐fold domain diminished the mast cell stimulatory activity, and the combinatorial substitutions L56F/K92E, L56F/D95S, and L56F/S100V abolished the stimulatory activities of the mutant that harbored OB‐fold domain of the active variant and the intact active variant. These indicate that the responsive elements of SSL12 for mast cell activation are in the OB‐fold of SSL12, and L56 would be an essential amino acid residue for the activation of mast cells. The findings would contribute to the understanding of the molecular mechanism of SSL12 for mast cell activation and the development of toxoids preventing allergic inflammations associated with Staphylococcus aureus.

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Section: Resultssupporting

confidence: 87%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Identification of responsible amino acid residues in staphylococcal superantigen‐like 12 for the activation of mast cells

et al. 2022

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“…Bacterial superantigens have also been reported to enhance MC activation, in some cases leading to degranulation, although impacts on cytokine production have been less well studied. Examples of these include enterotoxins A and B, and superantigen-like proteins (exotoxins) from S. aureus [82,83,84]. Bacterial toxins such as those derived from cholera, pertussis, and clostridium species have also been reported to be able to induce MC responses [85,86,87,113].…”

Section: Bacterial Pathogens and Productsmentioning

confidence: 99%

Mast Cell Responses to Viruses and Pathogen Products

Marshall

Portales‐Cervantes

Leong

2019

IJMS

124

133

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Mast cells are well accepted as important sentinel cells for host defence against selected pathogens. Their location at mucosal surfaces and ability to mobilize multiple aspects of early immune responses makes them critical contributors to effective immunity in several experimental settings. However, the interactions of mast cells with viruses and pathogen products are complex and can have both detrimental and positive impacts. There is substantial evidence for mast cell mobilization and activation of effector cells and mobilization of dendritic cells following viral challenge. These cells are a major and under-appreciated local source of type I and III interferons following viral challenge. However, mast cells have also been implicated in inappropriate inflammatory responses, long term fibrosis, and vascular leakage associated with viral infections. Progress in combating infection and boosting effective immunity requires a better understanding of mast cell responses to viral infection and the pathogen products and receptors we can employ to modify such responses. In this review, we outline some of the key known responses of mast cells to viral infection and their major responses to pathogen products. We have placed an emphasis on data obtained from human mast cells and aim to provide a framework for considering the complex interactions between mast cells and pathogens with a view to exploiting this knowledge therapeutically. Long-lived resident mast cells and their responses to viruses and pathogen products provide excellent opportunities to modify local immune responses that remain to be fully exploited in cancer immunotherapy, vaccination, and treatment of infectious diseases.

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“…To date, most of the published studies with ClearColi® BL21(DE3) have been restricted to complex medium formulations and shake flask cultures to produce enzymes (Liang et al 2015 ; An et al 2019 ; Jobin et al 2019 ; Song et al 2019 ), antigenic proteins (Martínez-Donato et al 2016 ; González-Miro et al 2017 ; Viranaicken et al 2017 ; Watkins et al 2017b , 2017a ; Abdellrazeq et al 2019 , 2020 ), and therapeutic products (Mamat et al 2015 ; Planesse et al 2015 ; Ueda et al 2016 ; Pooe et al 2017 ; Tomczak et al 2017 ; Wang et al 2017 ; Hunt et al 2019 ; Wilding et al 2019a , 2019b ; López et al 2021 ; Nguyen et al 2021 ). ClearColi® BL21(DE3) has also been used to produce diagnostic biomolecules (Masarapu et al 2017 ; Yoo et al 2017 ; Park et al 2021 ) and in specific functional studies (Moon et al 2018 ; Bong et al 2019 ; Hayashi et al 2019 ; Kobayashi et al 2019 ; Qiao et al 2019 ; Carratalá et al 2021 ; Hsu et al 2021 ; Segovia-Trinidad et al 2021 ), among other uses (Ran et al 2019 ; Sankaran et al 2019 ; Sankaran and del Campo 2019 ; Gnopo et al 2020 ). On the other hand, studies have demonstrated that the production of recombinant proteins in conventional E. coli cells is affected by several process factors (Kaur et al 2018 ) that may impact yields and titers, as well as lead to the formation of inclusion bodies and poor protein quality (Rosano and Ceccarelli 2014 ).…”

Section: Introductionmentioning

confidence: 99%

ClearColi as a platform for untagged pneumococcal surface protein A production: cultivation strategy, bioreactor culture, and purification

Cardoso

Paredes

Campani

et al. 2022

Appl Microbiol Biotechnol

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Several studies have searched for new antigens to produce pneumococcal vaccines that are more effective and could provide broader coverage, given the great number of serotypes causing pneumococcal diseases. One of the promising subunit vaccine candidates is untagged recombinant pneumococcal surface protein A (PspA4Pro), obtainable in high quantities using recombinant Escherichia coli as a microbial factory. However, lipopolysaccharides (LPS) present in E. coli cell extracts must be removed, in order to obtain the target protein at the required purity, which makes the downstream process more complex and expensive. Endotoxin-free E. coli strains, which synthesize a nontoxic mutant LPS, may offer a cost-effective alternative way to produce recombinant proteins for application as therapeutics. This paper presents an investigation of PspA4Pro production employing the endotoxin-free recombinant strain ClearColi® BL21(DE3) with different media (defined, auto-induction, and other complex media), temperatures (27, 32, and 37 °C), and inducers. In comparison to conventional E. coli cells in a defined medium, ClearColi presented similar PspA4Pro yields, with lower productivities. Complex medium formulations supplemented with salts favored PspA4Pro yields, titers, and ClearColi growth rates. Induction with isopropyl-β- d -thiogalactopyranoside (0.5 mM) and lactose (2.5 g/L) together in a defined medium at 32 °C, which appeared to be a promising cultivation strategy, was reproduced in 5 L bioreactor culture, leading to a yield of 146.0 mg PspA4Pro/g dry cell weight. After purification, the cell extract generated from ClearColi led to 98% purity PspA4Pro, which maintained secondary structure and biological function. ClearColi is a potential host for industrial recombinant protein production. Key points • ClearColi can produce as much PspA4Pro as conventional E. coli BL21(DE3) cells. • 10.5 g PspA4Pro produced in ClearColi bioreactor culture using a defined medium. • Functional PspA4Pro (98% of purity) was obtained in ClearColi bioreactor culture. Graphical abstract Supplementary Information The online version contains supplementary material available at 10.1007/s00253-022-11758-9.

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Staphylococcal superantigen-like 12 activates murine bone marrow derived mast cells

Cited by 11 publications

References 23 publications

Identification of responsible amino acid residues in staphylococcal superantigen‐like 12 for the activation of mast cells

Identification of responsible amino acid residues in staphylococcal superantigen‐like 12 for the activation of mast cells

Mast Cell Responses to Viruses and Pathogen Products

ClearColi as a platform for untagged pneumococcal surface protein A production: cultivation strategy, bioreactor culture, and purification

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