Characterization, phylogenetic analysis and cDNA cloning of natterin-like gene from the blood of lamprey, Lampetra japonica

Zhao, Xue; Liu, Xin; Pang, Yue; Yu, Tao; Xiao, Rong; Jin, Minli; Han, Yinglun; Su, Peng; Wang, Jihong; Lv, Li; Wu, Fenfang; Li, Qingwei

doi:10.1016/j.imlet.2012.08.005

Cited by 27 publications

(18 citation statements)

References 35 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Another homolog, the human ZG16p, exhibits high affinity toward the mannan of yeast and pathogenic fungi and has been suggested to attack the invading pathogens in the digestive system . Similar to its homologs in catfish and lamprey , Dln1 might be also a defense molecule in zebrafish, most likely via forming a transmembrane pore on the target cells similar to the previously reported mammal perforin‐2 .…”

Section: Discussionsupporting

confidence: 55%

“…Bioinformatic analysis revealed that the zebrafish Danio rerio encodes 16 hypothetical aerolysin‐like isoforms , which share a 55–98% sequence identity between isoforms over the full‐length protein of ~300 residues. Moreover, these isoforms share a sequence identity of ~60% to catfish and lamprey natterin‐like proteins, which are hypothetical defense molecules against predators . Here, we report the structures of one isoform (NCBI: NP_001013322.1), termed Dln1, in both water‐soluble dimeric form (at 1.86 Å) and membrane‐bound octameric form (at 20 Å) using X‐ray crystallography and electron microscopy (EM), respectively.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Structural basis for receptor recognition and pore formation of a zebrafish aerolysin‐like protein

et al. 2015

View full text Add to dashboard Cite

Various aerolysin-like pore-forming proteins have been identified from bacteria to vertebrates. However, the mechanism of receptor recognition and/or pore formation of the eukaryotic members remains unknown. Here, we present the first crystal and electron microscopy structures of a vertebrate aerolysin-like protein from Danio rerio, termed Dln1, before and after pore formation. Each subunit of Dln1 dimer comprises a b-prism lectin module followed by an aerolysin module. Specific binding of the lectin module toward high-mannose glycans triggers drastic conformational changes of the aerolysin module in a pH-dependent manner, ultimately resulting in the formation of a membrane-bound octameric pore. Structural analyses combined with computational simulations and biochemical assays suggest a pore-forming process with an activation mechanism distinct from the previously characterized bacterial members. Moreover, Dln1 and its homologs are ubiquitously distributed in bony fishes and lamprey, suggesting a novel fish-specific defense molecule.

show abstract

Section: Discussionsupporting

confidence: 55%

Section: Introductionmentioning

confidence: 99%

Structural basis for receptor recognition and pore formation of a zebrafish aerolysin‐like protein

et al. 2015

View full text Add to dashboard Cite

show abstract

“…Unknown function: Pore-forming toxins are the most common bacterial cytotoxic proteins and are required for virulence in a large number of important pathogens. Natterin-like protein is a pore-forming toxin with an unusually high toxicity and may be involved in the defense mechanism against specific predators in animals [ 33 ]. The functions of these two types of proteins have remained unclear in higher plants, but their transcription levels were greatly increased under biotic stress [ 34 ].…”

Section: Resultsmentioning

confidence: 99%

Physiological, Ultrastructural and Proteomic Responses in the Leaf of Maize Seedlings to Polyethylene Glycol-Stimulated Severe Water Deficiency

Shao

Xin

Mao

et al. 2015

IJMS

View full text Add to dashboard Cite

After maize seedlings grown in full-strength Hoagland solution for 20 days were exposed to 20% polyethylene glycol (PEG)-stimulated water deficiency for two days, plant height, shoot fresh and dry weights, and pigment contents significantly decreased, whereas malondialdehyde (MDA) content greatly increased. Using transmission electron microscopy, we observed that chloroplasts of mesophyll cells in PEG-treated maize seedlings were swollen, with a disintegrating envelope and disrupted grana thylakoid lamellae. Using two-dimensional gel electrophoresis (2-DE) method, we were able to identify 22 protein spots with significantly altered abundance in the leaves of treated seedlings in response to water deficiency, 16 of which were successfully identified. These protein species were functionally classified into signal transduction, stress defense, carbohydrate metabolism, protein metabolism, and unknown categories. The change in the abundance of the identified protein species may be closely related to the phenotypic and physiological changes due to PEG-stimulated water deficiency. Most of the identified protein species were putatively located in chloroplasts, indicating that chloroplasts may be prone to damage by PEG stimulated-water deficiency in maize seedlings. Our results help clarify the molecular mechanisms of the responses of higher plants to severe water deficiency.

show abstract

“…Sequence analysis indicated that these toxins are composed of a jacalin-like lectin domain linked to a toxic aerolysin domain. The family of nattering-like proteins with this AB-type structure has been reported in different fish (Xue et al 2012). Furthermore, blast searches in databases revealed that sequences encoding chimeric proteins containing Amaranthin-like domain(s) and an aerolysin-like domain are widespread in plants (Liuyi Dang, unpublished data).…”

Section: Ab Toxins Composed Of Lectin Domain(s) Linked To a Pore-formmentioning

confidence: 98%

Plant AB Toxins with Lectin Domains

Shang¹,

Dang²,

Damme³

2015

Plant Toxins

View full text Add to dashboard Cite

As part of their defense system different plant species each express a diverse set of defense proteins, among them proteins with lectin domains. The whole group of plant lectins assembles all proteins that have the ability to recognize and bind specific carbohydrate structures. Based on the sequence and the conformation of the carbohydrate recognition domains several lectin families are distinguished. Although many lectins are composed only of carbohydrate binding domains, several lectins are chimeric proteins composed of a lectin domain and another unrelated domain. In some cases this second domain can be considered as a toxin domain. This chapter focuses on different types of plant AB toxins and their physiological importance in the battle against pathogens and predators. Most information is available on type 2 ribosome-inactivating proteins in which an N-glycosidase domain is linked through a disulfide bridge to a lectin domain. More recently chimeric proteins consisting of one or more lectin domains and a dirigent domain or aerolysin domain have also been discovered. Although these AB toxins all consist of a lectin domain and a toxin domain, the nature of the toxin and the lectin domain are different resulting in proteins with different carbohydrate binding properties as well as a different mode of action for toxicity.

show abstract

Characterization, phylogenetic analysis and cDNA cloning of natterin-like gene from the blood of lamprey, Lampetra japonica

Cited by 27 publications

References 35 publications

Structural basis for receptor recognition and pore formation of a zebrafish aerolysin‐like protein

Structural basis for receptor recognition and pore formation of a zebrafish aerolysin‐like protein

Physiological, Ultrastructural and Proteomic Responses in the Leaf of Maize Seedlings to Polyethylene Glycol-Stimulated Severe Water Deficiency

Plant AB Toxins with Lectin Domains

Contact Info

Product

Resources

About