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Titolo:
Functional and structural diversities of C-reactive proteins present in horseshoe crab hemolymph plasma
Autore:
Iwaki, D; Osaki, T; Mizunoe, Y; Wai, SN; Iwanaga, S; Kawabata, S;
Indirizzi:
Kyushu Univ, Fac Sci, Dept Biol, Fukuoka 8128581, Japan Kyushu Univ Fukuoka Japan 8128581 Sci, Dept Biol, Fukuoka 8128581, Japan Kyushu Univ, Fac Med, Dept Bacteriol, Fukuoka 812, Japan Kyushu Univ Fukuoka Japan 812 ac Med, Dept Bacteriol, Fukuoka 812, Japan Kyushu Univ, Grad Sch Med Sci, Dept Mol Biol, Fukuoka 812, Japan Kyushu Univ Fukuoka Japan 812 Med Sci, Dept Mol Biol, Fukuoka 812, Japan
Titolo Testata:
EUROPEAN JOURNAL OF BIOCHEMISTRY
fascicolo: 2, volume: 264, anno: 1999,
pagine: 314 - 326
SICI:
0014-2956(199909)264:2<314:FASDOC>2.0.ZU;2-2
Fonte:
ISI
Lingua:
ENG
Soggetto:
GROUP-B STREPTOCOCCUS; CAPSULAR POLYSACCHARIDE ANTIGEN; ACID-SPECIFIC LECTIN; AMYLOID-P COMPONENT; LIMULUS-POLYPHEMUS; LOBSTER AGGLUTININS; PURIFICATION; BINDING; ALPHA(2)-MACROGLOBULIN; PENTRAXINS;
Keywords:
C-reactive protein; hemolysis; horseshoe crab; innate immunity; lectin;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
65
Recensione:
Indirizzi per estratti:
Indirizzo: Kawabata, S Kyushu Univ, Fac Sci, Dept Biol, Fukuoka 8128581, Japan KyushuUniv Fukuoka Japan 8128581 ol, Fukuoka 8128581, Japan
Citazione:
D. Iwaki et al., "Functional and structural diversities of C-reactive proteins present in horseshoe crab hemolymph plasma", EUR J BIOCH, 264(2), 1999, pp. 314-326

Abstract

Limulin, a sialic-acid-binding and phosphorylethanolamine-binding hemagglutinin in the hemolymph plasma of the American horseshoe crab (Limulus polyphemus), is a hemolytic C-reactive protein [Armstrong, P.B., Swarnakar, S., Srimal, S., Misquith, S., Hahn, E.A., Aimes, R.T. & Quigley, J.P. (1996) J. Biol. Chem. 271, 14717-14721]. We have now identified three types of C-reactive protein in the plasma of the Japanese horseshoe crab (Tachypleus tridentatus), based on different affinities against fetuin-agarose and phosphorylethanolamine-agarose determined by quantitative precipitin assays using fetuin and an artificial phosphorylethanolamine-protein conjugate. Partial amino acid sequences of the isolated C-reactive proteins identified homologous proteins which were named Tachypleus tridentatus CRP-1 (tCRP-1), tCRP-2 and tCRP-3, each of which possibly constitute isoprotein mixtures. tCRP-2 and tCRP-3, but not tCRP-1, agglutinated mammalian erythrocytes. tCRP-1, themost abundant C-reative protein in the plasma, exhibited the highest affinity to the phosphorylethanolamine-protein conjugate but locked both sialic-acid-binding and hemolytic activities. tCRP-2 bound to both fetuin-agarose and phosphorylethanolamine-agarose, and exhibited Ca2+-dependent hemolytic and sialic-acid-binding activities, suggestive of limulin-like properties, Furthermore, tCRP-2 exhibited a higher affinity to colominic acid, a bacterial polysialic acid. By contrast, tCRP-3 shows stronger hemolytic, sialic-acid-binding and hemagglutinating activities than tCRP-2. tCRP-3 has no affinity to phosphorylethsnolamine-agarose, phosphorylethanolamine-protein conjugate and colominic acid. This suggests tCRP-3 is a novel hemolytic C-reactive protein lacking a common characteristic of phosphorylethanolamine-agarose binding affinity. Twenty-two clones of tCRPs with different deduced amino acid sequences were obtained by PCR using oligonucleotide primers based on the N-terminal and C-terminal sequences of tCRPs and with templates including genomic DNA and cDNA of hemocytes or hepatopancreas derived from one individual, The translation products of the tCRP clones possess high molecular diversity which falls into three related groups, consistent with classification based on their biological activities. Only tCRP-3 contained a unique hydrophobic nonapeptide sequence that appears in the transmembrane domainof a major histocompatibility complex class I heavy chain of rainbow trout, suggesting the importance of the hydrophobic patch to the hemolytic activity of tCRP-3. The structural and functional diversities of tCRPs provide agood model for studying the properties of innate immunity in invertebrates, which survive without the benefit of acquired immunity.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 20/09/20 alle ore 06:53:06