Horseshoe Crab Hemocyte-derived Antimicrobial Polypeptides, Tachystatins, with Sequence Similarity to Spider Neurotoxins

Osaki, Tsukasa; Omotezako, Miyuki; Nagayama, Ranko; Hirata, Michimasa; Iwanaga, Sadaaki; Kasahara, Jiro; Hattori, Junji; Ito, Isao; Sugiyama, Hiroyuki; Kawabata, Shun Ichiro

doi:10.1074/jbc.274.37.26172

Cited by 103 publications

(91 citation statements)

References 43 publications

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“…However, these are very toxic for mammalian cells, since they cause hemolysis. The present results suggest that the bactericidal, fungicidal, and babesiacidal active sites are located in the Cterminal amino acid sequence, which consists of a ␤-sheet, in contrast to insect defensins, whose recognition site is located in an ␣-helix (38). Ticks are phylogenetically closer to spiders and scorpions (Arachnida, Chelicerata) than to insects (24,29).…”

Section: Discussionmentioning

confidence: 72%

Babesial Vector Tick Defensin againstBabesiasp. Parasites

et al. 2007

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Antimicrobial peptides are major components of host innate immunity, a well-conserved, evolutionarily ancient defensive mechanism. Infectious disease-bearing vector ticks are thought to possess specific defense molecules against the transmitted pathogens that have been acquired during their evolution. We found in the tick Haemaphysalis longicornis a novel parasiticidal peptide named longicin that may have evolved from a common ancestral peptide resembling spider and scorpion toxins. H. longicornis is the primary vector for Babesia sp. parasites in Japan. Longicin also displayed bactericidal and fungicidal properties that resemble those of defensin homologues from invertebrates and vertebrates. Longicin showed a remarkable ability to inhibit the proliferation of merozoites, an erythrocyte blood stage of equine Babesia equi, by killing the parasites. Longicin was localized at the surface of the Babesia sp. parasites, as demonstrated by confocal microscopic analysis. In an in vivo experiment, longicin induced significant reduction of parasitemia in animals infected with the zoonotic and murine B. microti. Moreover, RNA interference data demonstrated that endogenous longicin is able to directly kill the canine B. gibsoni, thus indicating that it may play a role in regulating the vectorial capacity in the vector tick H. longicornis. Theoretically, longicin may serve as a model for the development of chemotherapeutic compounds against tick-borne disease organisms.

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Section: Discussionmentioning

confidence: 72%

Babesial Vector Tick Defensin againstBabesiasp. Parasites

et al. 2007

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“…The data reported here suggest that the effect of the chitin-binding domain, in terms of amoebocyte recognition and phagocytosis, is relatively small; however, among invertebrates, chitin-binding domaincontaining proteins such as penaeidins in shrimp and tachycitins and tachystatins in the horseshoe crab hemocytes are essential for antifungal and antimicrobial activities (38)(39)(40). Chitin-binding domains also function in the detection of metazoan parasites (41).…”

Section: Discussionmentioning

confidence: 99%

A role for variable region-containing chitin-binding proteins (VCBPs) in host gut–bacteria interactions

Dishaw

Giacomelli²,

Melillo³

et al. 2011

Proc. Natl. Acad. Sci. U.S.A.

114

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A number of different classes of molecules function as structural matrices for effecting innate and adaptive immunity. The most extensively characterized mediators of adaptive immunity are the immunoglobulins and T-cell antigen receptors found in jawed vertebrates. In both classes of molecules, unique receptor specificity is effected through somatic variation in the variable (V) structural domain. V region-containing chitin-binding proteins (VCBPs) consist of two tandem Ig V domains as well as a chitin-binding domain. VCBPs are encoded at four loci (i.e., VCBPA-VCBPD) in Ciona, a urochordate, and are expressed by distinct epithelial cells of the stomach and intestine, as well as by granular amoebocytes present in the lamina propria of the gut and in circulating blood. VCBPs are secreted into the gut lumen, and direct binding to bacterial surfaces can be detected by immunogold analysis. Affinity-purified native and recombinant VCBP-C, as well as a construct consisting only of the tandem V domains, enhance bacterial phagocytosis by granular amoebocytes in vitro. Various aspects of VCBP expression and function suggest an early origin for the key elements that are central to the dialogue between the immune system of the host and gut microflora.bacteria opsonization | bacteria phagocytosis | immunoglobulin variable domains D ifferent molecular and cellular mechanisms that effect "innate" or "adaptive" immune responses shape immunity to pathogens such as viruses, bacteria, and parasites in all metazoans. The innate immune system includes germline-encoded receptor molecules that recognize widely divergent molecular structures. In contrast, the gene loci that encode the receptor molecules of the adaptive immune system undergo unique rearrangements in individual somatic cells that expand clonally and account for nearlimitless functional variation of receptors. The adaptive immune response is limited to jawed vertebrate species, whereas innate immunity is characteristic of all metazoan phyla.Alternative mechanisms of innate and adaptive immunity have been described in jawless vertebrates, protochordates, and other invertebrates (1, 2). Given the absence of V domain-mediated immunity in jawless vertebrates, the protochordate lineages are particular significant for understanding the origins of V region diversity as a basic form of immune recognition. In the protochordate Branchiostoma floridae (amphioxus), variable region-containing chitin-binding proteins (VCBPs) were described that consist of two variable (V) Ig domains and a single chitin-binding domain (3). VCBPs are encoded by diverse, nonrecombining, haplotypically variable alleles (4-6). Detailed structural studies of VCBPs reveal that the hyperpolymorphic positions are localized on the β-sheet surfaces of the folded V domains (7) and not on the connecting loops, which are the sites of the highest variability in the V domains of Ig and T-cell receptor (TCR). Other innate immune functions (e.g., viral receptor and superantigen-binding sites) are associated with V regi...

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“…Parker et al (1984) detected a hexapeptide with amino acid sequence of VEPIPY with immunostimulatory effect. The Miyata et al, 1989;Murakami et al, 1991;Ohta et al, 1992;Kawabata et al, 1996;Osaki et al, 1999 Blood of immune-challenged and untreated mussels (Mytilus edulis) peptide was claimed to stimulate in vitro phagocytosis of sheep red blood cells by murine macrophages and to have in vivo protective effect in mice against lethal infection caused by Klebsiella pneumonia (Parker et al, 1984). On the other hand, application of bioactive peptides from different resources has been limited due to their potential antigenicity and immunoreactivity in the body.…”

Section: Immunomodulatory Effectmentioning

confidence: 99%

Peptides: Production, bioactivity, functionality, and applications

Hajfathalian

Ghelichi

Moreno

et al. 2017

Critical Reviews in Food Science and Nutrition

138

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Production of peptides with various effects from proteins of different sources continues to receive academic attention. Researchers of different disciplines are putting increasing efforts to produce bioactive and functional peptides from different sources such as plants, animals, and food industry by-products. The aim of this review is to introduce production methods of hydrolysates and peptides and provide a comprehensive overview of their bioactivity in terms of their effects on immune, cardiovascular, nervous, and gastrointestinal systems. Moreover, functional and antioxidant properties of hydrolysates and isolated peptides are reviewed. Finally, industrial and commercial applications of bioactive peptides including their use in nutrition and production of pharmaceuticals and nutraceuticals are discussed.

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Horseshoe Crab Hemocyte-derived Antimicrobial Polypeptides, Tachystatins, with Sequence Similarity to Spider Neurotoxins

Cited by 103 publications

References 43 publications

Babesial Vector Tick Defensin againstBabesiasp. Parasites

Babesial Vector Tick Defensin againstBabesiasp. Parasites

A role for variable region-containing chitin-binding proteins (VCBPs) in host gut–bacteria interactions

Peptides: Production, bioactivity, functionality, and applications

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