Humoral immune responses of amphioxus Branchiostoma belcheri to challenge with Escherichia coli

Pang, Qiuxiang; Zhang, Shicui; Liu, Xuemei; Wu, Di

doi:10.1016/j.fsi.2005.11.001

Cited by 13 publications

(22 citation statements)

References 25 publications

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“…Interestingly, the secondary structure of GANL was also rather similar to that of CML, a mushroom lectin purified from ascomycete Cordyceps militaris (Jung et al 2007). However, there was no similarity in their N-terminal amino acid sequences (Jung et al 2007;Pang et al 2006;Pan et al 2010).…”

Section: Discussionmentioning

confidence: 99%

Structural characterization and antitumor and mitogenic activity of a lectin from the gill of bighead carp (Aristichthys nobilis)

Yao

Pan

Ming-qian

2012

Fish Physiol Biochem

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In this study, we investigated the gross structure, secondary structure, and antitumor and mitogenic activity of GANL, a lectin from the gill of bighead carp (Aristichthys nobilis). We used infrared spectroscopy, β-elimination, and circular dichroism spectroscopy to determine the structure of GANL. We measured antiproliferation activity against six human tumor cell lines and mitogenic activity against murine splenocytes using the MTT assay. Based on infrared spectroscopy and β-elimination, we conclude that GANL is a glycoprotein. The protein and carbohydrate moieties are joined by O-glycosidic linkage. A circular dichroism spectroscopic analysis revealed that the secondary structure of GANL consists of α-helices (34.8 %), β-sheets (12.1 %), β-turns (24.5 %), and unordered structures (33.0 %). GANL exerted potent antitumor activity against the HeLa cell line (IC(50) = 11.86 μg/mL) and a mitogenic effect on murine splenocytes in the MTT assay. GANL, a lectin that is isolated from the gills of bighead carp, is a glycoprotein with potent antitumor and mitogenic activity.

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Section: Discussionmentioning

confidence: 99%

Structural characterization and antitumor and mitogenic activity of a lectin from the gill of bighead carp (Aristichthys nobilis)

Yao

Pan

Ming-qian

2012

Fish Physiol Biochem

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“…Lysozyme activity was assayed as described by Minagawa et al (2001) with slight modifications (Pang et al 2004(Pang et al , 2006. Plates with 1.2 % agarose gels in 50 mM phosphate buffered solution (PBS; pH 5.0) containing 1 mg/ml Micrococcus lysodeikticus (M. lysodeikticus) were prepared.…”

Section: Lysozyme Assaymentioning

confidence: 99%

“…Inhibition of microbial growth by the humoral fluids was detected by colony forming unit (CFU) assay (Pang et al 2006;Zhang et al 2005), using the Gramnegative bacteria Escherichia coli (E. coli) or Vibrio alginolyticus (V. alginolyticus) and the Gram-positive bacteria Staphylococcus aureus (S. aureus) or Bacillus subtilis (B. subtilis) as the microbial targets. V. alginolyticus was cultured in 2216E medium at 26°C for 18 h. E. coli, S. aureus, and B. subtilis were both cultured in tryptic soy broth (TSB; Difco) at 37°C for 18 h. They were both collected at the logarithmic growth phase and suspended at a density of 5 9 10 3 cells/ml in 0.9 % NaCl solution.…”

Section: Assay Of Microbial Growth Inhibitionmentioning

confidence: 99%

“…Microbial agglutination by the humoral fluids was assayed according to the method of Pang et al (2006Pang et al ( , 2010 using the Gram-negative bacteria E. coli or V. alginolyticus and the Gram-positive bacteria S. aureus or B. subtilis as the targets. The microbes were cultured in tryptic soy broth (Difco) or in 2216E medium at 37 or 26°C for 18-24 h and harvested.…”

Section: Microbial Agglutination Assaymentioning

confidence: 99%

“…The humoral immune defense system in amphioxus plays an unexceptionally pivotal role in limiting microbial invasions and mediating the clearance or killing of invading microbes. Our previous investigation has shown that phenoloxidase activity, lysozyme activity, antimicrobial activity, microbial agglutinating activity, and hemagglutinating activity in the humoral fluids from amphioxus challenged with Escherichia coli and Vibrio alginolyticus significantly increased, which probably provides some degree of protection for the animals against invading microbes (Pang et al 2006(Pang et al , 2009(Pang et al , 2010. However, it needs further testing by LPS, which is common to all Gramnegative bacteria.…”

Section: Introductionmentioning

confidence: 99%

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Induction of phenoloxidase and other immunological activities in the humoral fluids of amphioxus Branchiostoma belcheri challenged with Lipopolysaccharide (LPS)

Pang

Liu

Zhao

et al. 2012

Fish Physiol Biochem

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An amphioxus gC1q protein binds human IgG and initiates the classical pathway: Implications for a C1q‐mediated complement system in the basal chordate

Gao

et al. 2014

Eur J Immunol

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The origin of the classical complement pathway remains open during chordate evolution. A C1q-like member, BjC1q, was identified in the basal chordate amphioxus. It is predominantly expressed in the hepatic caecum, hindgut, and notochord, and is significantly upregulated following challenge with bacteria or lipoteichoic acid and LPS. Recombinant BjC1q and its globular head domain specifically interact with lipoteichoic acid and LPS, but BjC1q displays little lectin activity. Moreover, rBjC1q can assemble to form the high molecular weight oligomers necessary for binding to proteases C1r/C1s and for complement activation, and binds human C1r/C1s/mannan-binding lectin-associated serine protease-2 as well as amphioxus serine proteases involved in the cleavage of C4/C2, and C3 activation. Importantly, rBjC1q binds with human IgG as well as an amphioxus Ig domain containing protein, resulting in the activation of the classical complement pathway. This is the first report showing that a C1q-like protein in invertebrates is able to initiate classical pathway, raising the possibility that amphioxus possesses a C1q-mediated complement system. It also suggests a new scenario for the emergence of the classical complement pathway, in contrast to the proposal that the lectin pathway evolved into the classical pathway.Keywords: Amphioxus r C1q r Classical complement pathway r IgG r IgSF Additional supporting information may be found in the online version of this article at the publisher's web-site IntroductionThe complement system, which helps Abs and phagocytic cells to clear pathogens from an organism, is a central component of innate immunity and a link between innate and adaptive immunity. The complement system is composed of more than 30 distinct plasma proteins and membrane-associated proteins that include Correspondence: Prof. Shicui Zhang e-mail: sczhang@ouc.edu.cn both effectors for foreign cell clearance and regulators for hostcell protection [1,2]. There are three pathways by which the complement system can be activated: the classical pathway, the lectin pathway, and the alternative pathway. Among them, the classical pathway is initiated by the binding of C1q, the first component of complement (C1), to immunoglobulins (IgG or IgM) within immune complexes, and its associated two serine proteases C1r and C1s, which leads to the subsequent cleavage of C4 and C2, followed by C3 activation [3]. From an evolutionary perspective, the classical complement pathway appears to have emerged only in the jaw vertebrates, when the adaptive immune system C 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim www.eji-journal.eu Eur. J. Immunol. 2014. 44: 3680-3695 Innate immunity 3681 was established in the cartilaginous lineage [4,5]. In the jawless fish lamprey, which lacks the conventional classical pathway, C1q is found to act as a lectin to bind N-acetyl-D-glucosamine (GlcNAc) and to initiate the complement system through the lectin pathway [6]. This has fueled the possibility that the lectin pathway evolved into the classical pat...

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Humoral immune responses of amphioxus Branchiostoma belcheri to challenge with Escherichia coli

Cited by 13 publications

References 25 publications

Structural characterization and antitumor and mitogenic activity of a lectin from the gill of bighead carp (Aristichthys nobilis)

Structural characterization and antitumor and mitogenic activity of a lectin from the gill of bighead carp (Aristichthys nobilis)

Induction of phenoloxidase and other immunological activities in the humoral fluids of amphioxus Branchiostoma belcheri challenged with Lipopolysaccharide (LPS)

An amphioxus gC1q protein binds human IgG and initiates the classical pathway: Implications for a C1q‐mediated complement system in the basal chordate

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