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Immunobiology
734
Reviews
VON ZABERN, I., HINSCH, B., PRZYKLENK, H., SCHMIDT, G. and VOGT, W. C o m p a r i s o n of Naja n. naja and Naja h. haje cobra-venom factors: correlation between binding affinity for the fifth component of complement and mediation of its cleavage. Immunobiology 157, 499 (1980). (Inge yon Zabern, Max-Planck-lnstitut ftir experimentelle Medizin, Department of Biochemical Pharmacology, 3400 G/Sttingen, FRG.) T w o COBRA-VENOM factors, one from Naja n. naja (CVF°), the other from Naja h. haje venom (CVF~'), have been purified and compared, functionally and structurally. Both factors interacted with h u m a n factors B and l) to form a potent C3 convertase, CVFBb. However, while the convertase formed with CVF n did also efficiently cleave C5, CVFhBb had very little CS-cleaving potency only, in particular when h u m a n C5 was used as substrate. Studies with agarose-linked CVF preparations indicated that CVF h has only low binding affinity for C5 ~p and C5 hu whereas CVF" binds to both C5 species with m u c h higher affinity. Since C5-binding (to CVF or to C3b) is a prerequisite for its cleavage by C 3 / C 5 convertases, the difference in binding potency explains the different C5-cleaving activity of the two CVF preparations. When a ligand for C5, surface-fixed C3b, is oresent, CVFhBb is also capable of cleaving C5. The difference in activities of CVF n and CVF h is reflected in their different potency to interfere with immune haemolysis and in causing indirect lysis by their complexes with activated factor B. By gel c h r o m a t o g r a p h y of the CVF preparations in CS-containing medium, a stoichiometric complex CVF"C5 (1 + 1) could be demonstrated. An analogous complex of C5 was neither found with CVF h, nor with C3 hu or soluble C3b hu. Structural differences between CVF" and CVF h were revealed by i m m u n o d i f f u s i o n analysis and by polyacrylamide-gel electrophoresis in the presence of SDS. The data available so far provide, however, no clear information about the structure of the C5 binding site. ( A u t h o r ' s abstract)
G. HABERMEHL
GORST-ALLMAN, C. P., MAES, C. M. T. P., RABIE, C. J. and STERN, P. S. 5, 6-Dihydro-4-methoxy-2Hpyran-2-one, a new mycotoxin from Penicillium italicum. S. Afr. J. Chem. 35, 102 (1982). (Charles P. GorstAllman, National Chemical Research Laboratory, CSIR, P.O. Box 395, Pretoria 0001, Republic of South Africa.) THE STRUCTURE of 5, 6-dihydro-4-methoxy-2H-pyran-2-one, a mycotoxin produced by Penicillium italicum, has been determined by spectroscopic methods. ( A u t h o r ' s abstract)
G. HABERMEHL
JOUBERT, F. J. Purification and some properties of a proteinase inhibitor (DE-3) from Erythrina humeana (dwarf erythrina) seed. S. Afr. J. Chem. 35, 67 (1982). (F. J. Joubert, National Chemical Research Laboratory, CSIR, P.O. Box 395, Pretoria 0001, Republic of South Africa). A PROTEINASE inhibitor (DE-3) was purified from Erythrina humeana seed by gel filtration on Sephadex G-50 followed by ion exchange chromatography on DEAE-cellulose and DEAE-sepharose. It contains 163 amino acids (molecular weight 17,900) including four half-cystine residues, and resembles the Kunitz-type proteinase inhibitors. The N-terminal primary structure of DE-3 also showed homology with those of the Kunitz-type inhibitors. Inhibitor DE-3 contains a potent inhibitor for both porcine trypsin and bovine a-chymotrypsin. ( A u t h o r ' s abstract)
G. HABERMEHL
MORRIS, J. G., el al. Ciguatera fish poisoning: epidemiology of the disease on St. T h o m a s , U. S. Virgin Islands. Am. J. trop. Med. Hyg. 3 1 , 5 7 4 (1982). (J. G. Morris, Centers for Disease Control, Enteritic Diseases Branch, Bacterial Diseases Division, Center for Infectious Diseases, Atlanta, GA 30333, U.S.A.) IN A RANDOM household survey conducted on St. T h o m a s , U.S. Virgin Islands, the incidence of ciguatera fish poisoning was found to be 36.5 cases per 1,000 population per 5 years (95°70 confidence limits _ 16.9 cases per 1,000 population per 5 years). An average of 3.6 cases per 1,000 population per year were diagnosed in the hospital emergency room on St. T h o m a s . Cases seen in the emergency room occurred most frequently a m o n g persons aged 30--39 years. No clear seasonality for cases could be demonstrated. In an investigation of cases occuring between I January and 10th April 1980, illness was caused by a variety of different fish, with carrang (Caranx tuber) the species most c o m m o n l y implicated. Patients a n d age-matched controls ate fish with equal frequency; patients were significantly more likely to have had previous episodes of ciguatera fish poisoning than were controls. ( A u t h o r ' s abstract)
G. HABERMEHL
Reviews
VON ZABERN, I., HINSCH, B., PRZYKLENK, H., SCHMIDT, G. and VOGT, W. C o m p a r i s o n of Naja n. naja and Naja h. haje cobra-venom factors: correlation between binding affinity for the fifth component of complement and mediation of its cleavage. Immunobiology 157, 499 (1980). (Inge yon Zabern, Max-Planck-lnstitut ftir experimentelle Medizin, Department of Biochemical Pharmacology, 3400 G/Sttingen, FRG.) T w o COBRA-VENOM factors, one from Naja n. naja (CVF°), the other from Naja h. haje venom (CVF~'), have been purified and compared, functionally and structurally. Both factors interacted with h u m a n factors B and l) to form a potent C3 convertase, CVFBb. However, while the convertase formed with CVF n did also efficiently cleave C5, CVFhBb had very little CS-cleaving potency only, in particular when h u m a n C5 was used as substrate. Studies with agarose-linked CVF preparations indicated that CVF h has only low binding affinity for C5 ~p and C5 hu whereas CVF" binds to both C5 species with m u c h higher affinity. Since C5-binding (to CVF or to C3b) is a prerequisite for its cleavage by C 3 / C 5 convertases, the difference in binding potency explains the different C5-cleaving activity of the two CVF preparations. When a ligand for C5, surface-fixed C3b, is oresent, CVFhBb is also capable of cleaving C5. The difference in activities of CVF n and CVF h is reflected in their different potency to interfere with immune haemolysis and in causing indirect lysis by their complexes with activated factor B. By gel c h r o m a t o g r a p h y of the CVF preparations in CS-containing medium, a stoichiometric complex CVF"C5 (1 + 1) could be demonstrated. An analogous complex of C5 was neither found with CVF h, nor with C3 hu or soluble C3b hu. Structural differences between CVF" and CVF h were revealed by i m m u n o d i f f u s i o n analysis and by polyacrylamide-gel electrophoresis in the presence of SDS. The data available so far provide, however, no clear information about the structure of the C5 binding site. ( A u t h o r ' s abstract)
G. HABERMEHL
GORST-ALLMAN, C. P., MAES, C. M. T. P., RABIE, C. J. and STERN, P. S. 5, 6-Dihydro-4-methoxy-2Hpyran-2-one, a new mycotoxin from Penicillium italicum. S. Afr. J. Chem. 35, 102 (1982). (Charles P. GorstAllman, National Chemical Research Laboratory, CSIR, P.O. Box 395, Pretoria 0001, Republic of South Africa.) THE STRUCTURE of 5, 6-dihydro-4-methoxy-2H-pyran-2-one, a mycotoxin produced by Penicillium italicum, has been determined by spectroscopic methods. ( A u t h o r ' s abstract)
G. HABERMEHL
JOUBERT, F. J. Purification and some properties of a proteinase inhibitor (DE-3) from Erythrina humeana (dwarf erythrina) seed. S. Afr. J. Chem. 35, 67 (1982). (F. J. Joubert, National Chemical Research Laboratory, CSIR, P.O. Box 395, Pretoria 0001, Republic of South Africa). A PROTEINASE inhibitor (DE-3) was purified from Erythrina humeana seed by gel filtration on Sephadex G-50 followed by ion exchange chromatography on DEAE-cellulose and DEAE-sepharose. It contains 163 amino acids (molecular weight 17,900) including four half-cystine residues, and resembles the Kunitz-type proteinase inhibitors. The N-terminal primary structure of DE-3 also showed homology with those of the Kunitz-type inhibitors. Inhibitor DE-3 contains a potent inhibitor for both porcine trypsin and bovine a-chymotrypsin. ( A u t h o r ' s abstract)
G. HABERMEHL
MORRIS, J. G., el al. Ciguatera fish poisoning: epidemiology of the disease on St. T h o m a s , U. S. Virgin Islands. Am. J. trop. Med. Hyg. 3 1 , 5 7 4 (1982). (J. G. Morris, Centers for Disease Control, Enteritic Diseases Branch, Bacterial Diseases Division, Center for Infectious Diseases, Atlanta, GA 30333, U.S.A.) IN A RANDOM household survey conducted on St. T h o m a s , U.S. Virgin Islands, the incidence of ciguatera fish poisoning was found to be 36.5 cases per 1,000 population per 5 years (95°70 confidence limits _ 16.9 cases per 1,000 population per 5 years). An average of 3.6 cases per 1,000 population per year were diagnosed in the hospital emergency room on St. T h o m a s . Cases seen in the emergency room occurred most frequently a m o n g persons aged 30--39 years. No clear seasonality for cases could be demonstrated. In an investigation of cases occuring between I January and 10th April 1980, illness was caused by a variety of different fish, with carrang (Caranx tuber) the species most c o m m o n l y implicated. Patients a n d age-matched controls ate fish with equal frequency; patients were significantly more likely to have had previous episodes of ciguatera fish poisoning than were controls. ( A u t h o r ' s abstract)
G. HABERMEHL