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3. National scientific medical meeting 1995 abstracts: Oral presentations

Author

Norris, S., Collins, C., Hegarty, J., O’Farrelly, C., Carton, J., Madrigal, L., O’Donoghue, D. P., O’Farrelly, C., Holloway, H., Fielding, J. F., Mullins, W., Hone, S. W., Donnelly, M., Powell, F., Blayney, A. W., Cahill, E. A., Daly, S. F., Turner, M. J., Sullivan, P. A., McLoughlin, M., Skelly, M. M., Mulcahy, H. E., Connell, T., O’Donoghue, D. P., Duggan, C., Duffy, M. J., Troy, A., Sheahan, K., Whelan, A., Herra, C. M., Keane, C. T., Johnson, H., Lee, B., Doherty, E., McDonnell, T., Mulherin, D., FitzGerald, O., Bresnihan, B., Hassett, H. M., Boyce, A., Greig, V., O’Herlihy, C., Smyth, P. P. A., Roche, E. F., McCormack, I., Tempany, E., Cullen, M. J., Smith, D. F., Smyth, P. P. A., McBrinn, Y., Murray, B., Freaney, R., Keating, D., McKenna, M. J., O’Hare, J. A., Alam, H., Raza, Q., Geoghegan, M., Killalea, S., Hall, M., Feely, J., Kyne, L., O’Hara, B., Cullen, M., Rea, I. M., Donnelly, J. P., Stout, R. W., Lacey, P., Donnelly, M. J., McGrath, J., Hennessy, T. P., Timon, C. V. I., Hyde, D., Xia, H. X., Keane, C. T., Buckley, M., O’Morain, C., Buckley, M., Keating, S., Xia, H., Hyde, D., O’Morain, C., McGrath, J. P., Stuart, R. C., Lawlor, P., Byrne, P. J., Walsh, T. N., Hennessy, T. P. J., Skelly, M. M., Mulcahy, H. E., Connell, T., O’Donoghue, D. P., Duggan, C., Duffy, M., Troy, A., Sheahan, K., Norris, S., Tubridy, M., Redmond, J., Hegarty, J., Holloway, H., Fielding, J. F., Mullins, W., Monahan, K., Murphy, R. P., Headon, D. R., O’Gorman, T., O’Reilly, F. M., Darby, C., Fielding, J. F., Murphy, G. M., Murphy, A., Codd, M., Powell, F., Dervan, P., Lawlor, D., Loughlin, S. O., Flanagan, N., Watson, R., Barnes, L., Flanagan, N., Watson, R., Kilgallen, C., Sweeney, E., Mynes, A., Mooney, D., Donoghue, I., Browne, O., Kirrane, J. A., Murphy, G. M., McKenna, D., Young, M., McKenna, D., Young, M., O’Toole, E., Young, M., O’Briain, S., Srinivasan, U., Feighery, C., Leonard, N., Jones, E., O’Farrelly, C., Moloney, M. A., O’Farrelly, C., Weir, D. G., Lawler, M., O’Neill, A., Gowing, H., Pamphilon, D., McCann, S. R., O’Toole, G., Orren, A., Seifer, C. M., Crowley, D. C., Sheehan, G. J., Deignan, T., Kelly, J., O’Farrelly, C., Tormey, V. J., Faul, J., Leonard, C., Burke, C. M., Poulter, L. W., Collins, C., Lynch, S., Madrigal, L., Norris, S., McEntee, G., Traynor, O., Hegarty, J., O’Farrelly, C., Barry, E., Collins, C., Costello, P., Keavney, A., O’Donoghue, D. P., O’Farrelly, C., Willoughby, R., Feighery, C., O’Donnell, C., Cahill, M., Earley, A., Eustace, P., Osborne, R., Cahill, M., Saidlear, C., Holmes, B., Early, A., Eustace, P., Moran, A. P., Neisser, A., Polt, R. J., Bernheimer, H., Kainz, M., Schwerer, B., Gallagher, L., Cahill, M., Saidlear, C., Early, A., Firth, R., Eustace, P., Kennedy, N., McGilloway, E., Redmond, J., McGilloway, E., Kennedy, N., Tubridy, N., Shields, K., Cullen, W. K., Rowan, M. J., Moore, A. R., Rowan, M., Feely, J., Coakley, D., Lawlor, B., Swanwick, G., Al-Naeemi, R., Redmond, J., Murphy, R., Feely, J., Codd, N. M., Goggins, M., Kennedy, N. P., Mallon, B. L., Kennedy, N. P., Mulherin, D., FitzGerald, O., Bresnihan, B., Mulcahy, H., Skelly, M., Donoghue, D. O., McCarthy, D., Saunders, A., Mulherin, D., Bresnihan, B., FitzGerald, O., Veale, D. J., Belch, J. J. F., Mulherin, D., Bresnihan, B., FitzGerald, O., Veale, D. J., Belch, J. J. F., Mulherin, D., FitzGerald, O., Bresnihan, B., Costello, P., Breathnach, D., Murphy, E., Mulherin, D., FitzGerald, O., Bresnihan, B., Breathnach, D., Costello, P., Mulherin, D., Bresnihan, B., FitzGerald, O., Breathnach, D., Mulherin, D., Costello, P., Bresnihan, B., FitzGerald, O., Kernohan, G., Gibson, K., Wilson, A. G., Duff, G. W., de Vries, N., van de Putte, L. B. A., Donoghue, J., O’Kelly, F., Johnson, Z., Maher, T., Kyne, L., Moran, A., Keane, C., O’Neill, D., Horgan, N., Barragry, J. M., O’Neill, D., O’Herlihy, C., Campbell, D. M., Behan, M., O’Connell, P. R., Donnelly, V. S., Crowley, D., Geary, M., Boylan, P., Geary, M., Fanagan, M., Boylan, P., Hickey, K., Teoh, T., Doyle, M., Harrison, R., Hickey, K., Lyons, D., Shenouda, Y., Coughlan, M., McKenna, P., Hickey, K., Shenouda, Y., Lyons, D., McKenna, P., Coughlan, M., Lenehan, P., Foley, M., Kelehan, P., Ravichandran, P., Kelly, M., Conroy, A., Fitzpatrick, C., Egan, D., Regan, C. L., McAdam, B. V., McParland, P., Boylan, P., FitzGerald, G. A., Fitzgerald, D. J., Sharma, S. C., Foran, K., Barry-Kinsella, C., Harrison, R. F., Gillespie, F. J., O’Mahony, P., Boyle, M., White, M. J., Donohoe, F., Birrane, Y., Naughton, M., Tempany, E., Fitzsimons, R. B., Piracha, M., McConkey, S., Griffin, E., Hayes, E., Clarke, T., Parfrey, N., Butler, K., Fitzpatrick, C., Malone, A. J., Kearney, P. J., Duggan, P. F., Lane, A., Keville, R., Turner, M., Barry, S., Sloan, D., Gallagher, S., Darby, M., Galligan, P., Stack, J., Walsh, N., O’Sullivan, M., Fitzgerald, M., O’Sullivan, M., Meagher, D., Sloan, D., Browne, S., Meagher, D., Larkin, C., Lane, A., Casey, P., O’Callaghan, E., Walsh, N., Rooney, S., Walsh, E., Morris, M., Lane, A., Burke, T., Larkin, C., O’Callaghan, E., Browne, S., Roe, M., Lane, A., Larkin, C., O’Callaghan, E., Maher, C., Wrigley, M., Gill, M., Burgess, M., Corcoran, E., Walsh, D., Gilmer, B., Johnson, H., Hayes, C. B., Thornton, L., Fogarty, J., Lyons, R., O’Connor, M., Delaney, V., Buckley, K., Johnson, Z., Johnson, Z., Lillis, D., Delany, V., Hayes, C., Dack, P., Igoe, D., Gilmer, B., O’Neill, H. J., Johnson, H., Igoe, D., Delaney, V., Johnson, Z., Kelly, P., McKeown, D., Clancy, L., Varghese, G., Hennessy, S., Codd, M., Gilmartin, J. J., Birthistle, K., Carrington, D., Maguire, H., Atkinson, P., Foley-Nolan, C., Lynch, M., Cryan, B., Whyte, D., Cryan, B., Conlon, C., Foley-Nolan, C., Johnson, Z., Hayes, C., Delany, V., Kucinskas, V., Usinskiene, U., Sakalyte, I., Johnson, Z., Hayes, C., Delaney, V., Dack, P., Gill, M., Dawson, E., Molloy, K., Goulden, N., Lawler, M., McCann, S. R., Doyle, J., Lawlor, E., Lawler, M., Harrington, M. G., El-Nageh, N., Nolan, M. -L., El-Nageh, N., Nolan, M. -L., Harrington, M. G., Lawlor, E., O’Riordan, J., McCann, S. R., Judge, G., Crotty, G., Finch, T., Borton, M., Barnes, T., Gilligan, O., Lee, G., Limmer, R., Madden, M., Whyte, D., Cryan, B., Bergin, C., O’Leary, A., Keating, S., Mulcahy, F., Wallis, F., Glennon, M., Cormican, M., NiRiain, U., Heiginbothom, M., Gannon, F., Smith, T., O’Sullivan, C., Hone, R., Orren, A., Caugant, D. A., Fijen, C. A. P., Van Schalkwyk, E. J., Coetzee, G. J., Lynch, M., Cryan, B., Riain, U. Ni, Cormican, M. G., Park, L., Flynn, J., Glennon, M., O’Connor, M., Regazzoli, V., O’Connor, M., Hayes, M., Nicholson, G., Higgins, P., NiRiain, U., Flynn, N., Corbett-Feeney, G., Conway, D. J., Sheahan, K., O’Higgins, N. J., Smyth, P. P. A., Rajendiran, S., Byrne, J., Kilfeather, E., Dingle, P., Hunter, M., Kelehan, P., Al-Ghazal, S. K., Stanley, P., Palmer, J., Hong, A., Al-Ghazal, S. K., Saxby, P., Al-Ghazal, S. K., Saxby, P., McConkey, S., Sheehan, D., Regan, I., O’Mullane, J., Chaoimh, M. Ni, Leahy, M., Heffron, J. J., Lehane, M., Keohane, C., O’Leary, N., Sheehan, M., Renny-Walsh, E., Whelton, M. J., Doyle, C. T., Webster, J., Benjamin, N., Lyons, D., FitzGerald, S., Chadha, J. S., FitzGerald, M. G., FitzGerald, G. R., Hemeryck, L., McGettigan, P., Feely, J., McGettigan, P., Feely, J., McGettigan, P., Golden, J., Feely, J., Arthur, N., Wen, S. Y., Killalea, S., Deegan, P., McGettigan, P., Feely, J., Cooke, T., Adebayo, G. I., Feely, J., Gaffney, P., Sinnot, M., O’Riordan, D., Hayes, T., O’Connor, C. M., FitzGerald, M. X., Costello, C., Finlay, G., Hayes, J., O’Connor, C., FitzGerald, M. X., McMahon, K., O’Farrelly, C., O’Connor, C., FitzGerald, M. X., Donnelly, M. J., Hone, S., Robertson, J., Coakley, R., O’Neill, S., Walsh, M., McCarthy, J., Lannon, D., Wood, A. E., Sharkey, R., Mulloy, E., Long, M., Kilgallen, I., O’Neill, S., Faul, J., Tormey, V., Leonard, C., Burke, C. M., Poulter, L. W., Horne, S., Tormey, V. J., Faul, J., Leonard, C., Burke, C. M., Feeney, T., Muiré, Ó. Ó, Gilmartin, J. J., Griffin, M. J., Hughes, D., Knaggs, A., Magee, D., Donnelly, M., McCrory, C., March, B., Hone, R., Phelan, D., White, M., Fabry, J., Lynch, M., Buggy, D., Cooney, C., Hughes, D., McCrory, C., Aziz, E., O’Herlihy, C., Kelly, J., O’Keefe, D., McShane, A. J., Boylan, J., Tobin, E., Smith, T., Motherway, C., Colreavy, F., Denish, N., Dwyer, R., Bergin, A., O’Brien, K., MacSullivan, R., Carson, K. D., Blunnie, W. P., Moriarty, D. C., Carson, K. D., Blunnie, W. P., Moriarty, D. C., Kinirons, B., Lyons, B., Cregg, N., Casey, W., Moore, K. P., Colbert, S. A., Ecoffey, C., O’Gorman, D., Fitzgerald, J., Phelan, D., Diamond, P., Codd, M. B., Sugrue, D. D., Kellett, J., Tighe, M., McKenna, C. J., Galvin, J., McCann, H. A., Sugrue, D. D., McKenna, C. J., Codd, M. B., McCann, H. A., Sugrue, D. D., Scallon, A., Buckley, M., Fraser, A., Norton, M., Tomkin, G., Graham, I., Byrne, A., Maher, M., Moran, N., Fitzgerald, D., O’Callaghan, D., Coyle, D., Nugent, A. G., McGurk, C., Johnston, G. D., McGurk, C., Nugent, A., Silke, B., Nugent, A. G., Johnston, G. D., Murphy, N., Jennings, L., Pratico, D., Doyle, C., Fitzgerald, D., Hennessy, T., McCann, H., Sugrue, D., Hennessy, T., Codd, M., Donnelly, S., Hennessy, A., Hartigan, C., McCann, H., Sugrue, D., Hennessy, T., Codd, M., Donnelly, S., Hennessy, A., Hartigan, C., McCann, H., Sugrue, D., Hennessy, T., MacDonald, D., Blake, S., McCann, H., Sugrue, D., Hennessy, T., Sugrue, D., McCann, H., Hennessy, T., McCann, H., Sugrue, D., Hennessy, T., McDonald, D., Blake, S., Dominque, D., Sugrue, D., McMechan, S. R., MacKenzie, G., Allen, J., Wright, G. T., Dempsey, G. J., Crawley, M., Anderson, J., Adgey, A. A. J., Harbinson, M. T., Campbell, N. P. S., Wilson, C. M., Ellis, P. K., McIlrath, E. M., Freaney, R., McShane, A., Keaveny, T. V., McKenna, M. J., Rabenstein, K., Scheller, F., Pfeiffer, D., Urban, C., Moser, I., Jobst, G., Manz, A., Verpoorte, S., Dempsey, F., Diamond, D., Smyth, M., Rabenstein, K., Dempsey, E., McShane, A., Keaveny, T. V., McKenna, M. J., Freaney, R., Hamilton, V., Dwyer, R., Twomey, J., Crowley, R., Fenelon, L., Walsh, F., McCann, J., McDonagh, P., White, M., McGovern, E., Luke, D., Phelan, D., McCrory, C., Crowley, K., Lyons, B., Mannion, D., Wood, A. E., Casey, W., Murphy, D., Clarkson, K., Carton, E., Higgins, P., Leonard, I., O’Toole, D., Staunton, M., Phelan, D., Srinivasan, U., Leonard, N., Jones, E., Moloney, M. A., Weir, D. G., O’Farrelly, C., Feighery, C., Griffin, M., Owens, D., Collins, P., Johnson, A., Tomkin, G. H., Herity, N. A., Allen, J. D., Silke, B., Adgey, A. A. J., O’Reilly, F. M., Darby, C., O’Moore, R., Fielding, J. F., Murphy, G. M., Crotty, G. M., Judge, G., McCann, S. R., DeArce, M., Nugent, A. G., McGurk, C., Johnston, G. D., Nikookam, K., Keenan, P., Cregan, D., Firth, R., O’Meara, N., Forman, S., Cusack, D. A., and Farrell, B.

Published
1995
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7. Precision and accuracy of single-molecule FRET measurements - a multi-laboratory benchmark study

Author

Hellenkamp, B., Schmid, S., Doroshenko, O., Opanasyuk, O., Kühnemuth, R., Adariani, S.R., Barth, A., Birkedal, V., Bowen, M.E., Chen, H., Cordes, T., Eilert, T., Fijen, C., Götz, M., Gouridis, G., Gratton, E., Ha, T., Hanke, C.A., Hartmann, A., Hendrix, J., Hildebrandt, L.L., Hohlbein, J., Hübner, C.G., Kallis, E., Kapanidis, A.N., Kim, J.-Y., Krainer, G., Lamb, D.C., Lee, N.K., Lemke, E.A., Levesque, B., Levitus, M., McCann, J.J., Naredi-Rainer, N., Nettels, D., Ngo, T., Qiu, R., Röcker, C., Sanabria, H., Schlierf, M., Schuler, B., Seidel, H., Streit, L., Tinnefeld, P., Tyagi, S., Vandenberk, N., Weninger, K.R., Wünsch, B., Yanez-Orozco, I.S., Michaelis, J., Seidel, C.A.M., Craggs, T.D., and Hugel, T.

Abstract

Single-molecule Förster resonance energy transfer (smFRET) is increasingly being used to determine distances, structures, and dynamics of biomolecules in vitro and in vivo. However, generalized protocols and FRET standards to ensure the reproducibility and accuracy of measurements of FRET efficiencies are currently lacking. Here we report the results of a comparative blind study in which 20 labs determined the FRET efficiencies (E) of several dye-labeled DNA duplexes. Using a unified, straightforward method, we obtained FRET efficiencies with s.d. between ±0.02 and ±0.05. We suggest experimental and computational procedures for converting FRET efficiencies into accurate distances, and discuss potential uncertainties in the experiment and the modeling. Our quantitative assessment of the reproducibility of intensity-based smFRET measurements and a unified correction procedure represents an important step toward the validation of distance networks, with the ultimate aim of achieving reliable structural models of biomolecular systems by smFRET-based hybrid methods.

Published
2018

13. A single-molecule FRET sensor for monitoring DNA synthesis in real time

Author

Fijen, C., Monton Silva, Alejandro, Hochkoeppler, Alejandro, Hohlbein, J.C., Fijen, C., Monton Silva, Alejandro, Hochkoeppler, Alejandro, and Hohlbein, J.C.

Abstract

We developed a versatile DNA assay and framework for monitoring polymerization of DNA in real time and at the single-molecule level. The assay consists of an acceptor labelled DNA primer annealed to a DNA template that is labelled on its single stranded, downstream overhang with a donor fluorophore. Upon extension of the primer using a DNA polymerase, the overhang of the template alters its conformation from a random coil to the canonical structure of double stranded DNA. This conformational change increases the distance between the donor and the acceptor fluorophore and can be detected as a decrease in the Förster resonance energy transfer (FRET) efficiency between both fluorophores. Remarkably, the DNA assay does not require any modification of the DNA polymerase and albeit the simple and robust spectroscopic readout facilitates measurements even with conventional fluorimeters or stopped-flow equipment, single-molecule FRET provides additional access to parameters such as the processivity of DNA synthesis and, for one of the three DNA polymerases tested, the detection of binding and dissociation of the DNA polymerase to DNA. We furthermore demonstrate that primer extensions by a single base can be resolved.

Published
2017

14. A Nanofluidic Mixing Device for High-throughput Fluorescence Sensing of Single Molecules

Author

Mathwig, Klaus, Fijen, C., Fontana, M., Lemay, S.G., Hohlbein, J.C., Mathwig, Klaus, Fijen, C., Fontana, M., Lemay, S.G., and Hohlbein, J.C.

Abstract

We introduce a nanofluidic mixing device entirely fabricated in glass for the fluorescence detection of single molecules. The design consists of a nanochannel T-junction and allows the continuous monitoring of chemical or enzymatic reactions of analytes as they arrive from two independent inlets. The fluorescently labeled molecules are tracked before, during and after they enter the mixing region, and their reactions with each other are observed by means of optical readout such as Förster Resonance Energy Transfer (FRET). Our method can be used for analyzing the kinetics of DNA annealing in a high-parallelized fashion.

Published
2017

17. Comparison of commercial diagnostic tests for identification of serogroup antigens of Neisseria meningitidis

Author

van der Ende, A., Schuurman, I. G., Hopman, C. T., Fijen, C. A., Dankert, J., and Other departments

Abstract

In the study that is described the sensitivities and specificities of three commercial tests and the standard Reference Laboratory test, used since 1961, to identify Neisseria meningitidis serogroups were compared. The tests marketed by Difco, Murex/Wellcome, and Sanofi/Pasteur showed overall sensitivities of 92, 95, and 100%, respectively, and specificities of 67, 88, and 82%, respectively. When limited to the common serogroups A, B, and C, the three tests yielded sensitivities of 93, 97, and 100%, respectively, and specificities of 98, 100, and 98%, respectively. However, determination of the uncommon serogroups X, W-135, Y, Z, and 29E with these tests is either unreliable or not possible

Published
1995

18. Role of neutrophil Fc gamma RIIa (CD32) and Fc gamma RIIIb (CD16) polymorphic forms in phagocytosis of human IgG1- and IgG3-opsonized bacteria and erythrocytes

Author

Bredius, R G, Fijen, C A, De Haas, M, Kuijper, E J, Weening, R S, Van de Winkel, J G, and Out, T A

Subjects
Erythrocytes, Rosette Formation, Bacteria, Phagocytosis, Antigens, CD, Neutrophils, Immunoglobulin G, Rho(D) Immune Globulin, Receptors, IgG, Humans, Opsonin Proteins, Cells, Cultured, Research Article
Abstract

The four subclasses of IgG have different biological activities associated with their Fc regions. Fc gamma receptors on leucocytes (Fc gamma R) mediate binding and phagocytosis of opsonized particles. Two structurally and functionally distinct allelic polymorphisms of the Fc gamma R have been defined: the H/R131 forms of Fc gamma RIIa (CD32), and the neutrophil antigen 1 (NA1)/NA2 forms of Fc gamma RIIIb (CD16). In this study the activities of allotypes of CD16 are analysed with antibacterial IgG subclass antibodies and with IgG1 and IgG3 anti-Rhesus D, and the activities of CD32 with IgG1 and IgG3 anti-Rhesus D. With respect to the allotypes of CD16, polymorphonuclear leucocytes (PMN) homozygous for Fc gamma RIIb-NA2 exhibited a lower (21-25%) IgG1-mediated phagocytosis of Staphylococcus aureus strain Wood (STAW), Haemophilus influenzae type b (Hib), and Neisseria meningitidis group B (NMen) than IIIb-NA1 PMN. The difference was apparent only when the micro-organisms were opsonized in the absence of complement, and was furthermore enhanced (34-52%) upon blockade of Fc gamma RIIa. In addition, monoclonal IgG3 anti-D-mediated rosette formation and phagocytosis was consistently found to be lower (16%) with Fc gamma RIIIb-NA2 than with IIIb-NA1 PMN. For the allotypes of CD32 we now show that IgG3 anti-D sensitized erythrocytes formed more (50%) rosettes and were phagocytosed at a higher rate with PMN carrying Fc gamma RIIa-H131 than with PMN carrying IIa-R131. Heterozygous Fc gamma RIIa-H/R131 PMN exhibited intermediate phagocytic activity in this respect. This study illustrates a critical role of Fc gamma R allotypes in functional interactions with biologically relevant IgG subclass antibodies.

Published
1994

19. Fc gamma receptor IIa (CD32) polymorphism in fulminant meningococcal septic shock in children

Author

Bredius, R. G., Derkx, B. H., Fijen, C. A., de Wit, T. P., de Haas, M., Weening, R. S., van de Winkel, J. G., Out, T. A., and Other departments

Abstract

Antibodies are essential in host defense against Neisseria meningitidis. Therefore, interactions among IgG and Fc receptors (Fc gamma R) on phagocytes may be crucial. Genetic polymorphic forms of Fc gamma RIIa (CD32) express different functional activities. In a retrospective study, Fc gamma R polymorphisms were determined in 25 children who survived fulminant meningococcal septic shock: 11 had Fc gamma RIIa-R/R131, the poor IgG2-binding allotype, which is a significantly more frequent rate than found in a healthy white population (44% vs. 23%; P = .028; odds ratio = 2.67; 95% confidence interval, 1.09-6.53). The relevance of this finding was further supported by the fact that neutrophils with the Fc gamma RIIa-R/R131 allotype phagocytized N. meningitidis opsonized with polyclonal IgG2 antibodies less effectively than did IIa-H/H131 neutrophils. Our findings suggest an important role for anti-N. meningitidis IgG2 and the Fc gamma RIIa polymorphism in host defense against systemic meningococcal infections

Published
1994

31. Fulminant meningococcal septic shock in a boy with combined inherited properdin and protein C deficiency.

Author

Fijen, C. A. P., Derkx, B. H. F., Kuijper, E. J., Mannens, M., Poort, S. R., Peters, M., Daha, M. R., and Dankert, J.

Subjects
*NEISSERIA meningitidis, *PULMONARY embolism, *ARTERIAL occlusions, *ENZYME activation, *DNA polymerases, *POLYMERASE chain reaction
Abstract

A 7-year-old patient with fulminant septic shock, due to Neisseria meningitidis of the uncommon serogroup Y developed extensive gangrene of the limbs. Multiple amputations were necessary and a pulmonary embolism occurred within 2 days post-operatively. Complement and haemostatic system studies, done after recovery, showed a complete absence of properdin antigen and a low protein C antigen and activity level in plasma. Defective haemolytic activity in gel by the alternative pathway of complement activation could be restored with purified properdin, indicating a properdin deficiency type I. Protein C antigen level as well as activity were in agreement with a protein C deficiency type 1. The polymerase chain reaction (PCR) product of exon five of the protein C gene showed a substitution of 72Gly by Arg. Both deficiencies were traced among relatives of the patient. Serum of the father of the patient's mother was also properdin-deficient. Microsatellite haplotyping of the X-chromosome of the patient and his relatives showed that a distinct haplotype cosegregated with the properdin deficiency (Lodscore 2.25; four informative meioses). The protein C type I deficiency was present in the patient's mother and her mother and cosegregated with the mutation found. So far as is known, this is the first patient described with combined inherited properdin deficiency and protein C deficiency. [ABSTRACT FROM AUTHOR]

Published
1995

32. Role of neutrophil FcγRIIa (CD32) and FcγRIIIb (CD16) polymorphic forms in phagocytosis of human IgG1- and IgG3-opsonized bacteria and erythrocytes.

Author

Bredius, R. G. M., Fijen, C. A. P., De Haas, M., Kuijper, E. J., Weening, R. S., Vande Winkel, J.G.J., and Out, T.A.

Subjects
*NEUTROPHILS, *PHAGOCYTES, *LEUCOCYTES, *PHAGOCYTOSIS, *ERYTHROCYTES, *BACTERIA
Abstract

The four subclasses of IgG have different biological activities associated with their Fc regions. Fcγ receptors on leucocytes (FcγR) mediate binding and phagocytosis of opsonized particles. Two structurally and functionally distinct allelic polymorphisms of the FcγR have been defined: the H/R131 forms of FcγRIIa (CD32), and the neutrophil antigen 1 (NA1)/NA2 forms of FcγRIIIb (CD16). In this study the activities of allotypes of CD16 are analysed with antibacterial IgG subclass antibodies and with IgG 1 and IgG3 anti-Rhesus D, and the activities of CD32 with IgG1 and IgG3 anti-Rhesus D. With respect to the allotypes of CD16, polymorphonuclear leucocytes (PMN) homozygous for FcγRIIIb-NA2 exhibited a lower (21-25%) IgG1-mediated phagocytosis of Staphylococcus aureus strain Wood (STAW), Haemophilus influenzae type b (Hib), and Neisseria meningitidis group B (NMen) than IIIb-NA1 PMN. The difference was apparent only when the micro-organisms were opsonized in the absence of complement, and was furthermore enhanced (34-52%) upon blockade of FcγRIIa. In addition, monoclonal IgG3 anti-D-mediated rosette formation and phagocytosis was consistently found to be lower (16%) with FcγRIIIb-NA2 than with IIIb-NA1 PMN. For the allotypes of CD32 we now show that IgG3 anti-D sensitized erythrocytes formed more (50%) rosettes and were phagocytosed at a higher rate with PMN carrying FcγRIIa-H131 than with PMN carrying IIa-R131. Heterozygous FcγRIIa-H/R131 PMN exhibited intermediate phagocytic activity in this respect. This study illustrates a critical role of FcγR allotypes in functional interactions with biologically relevant IgG subclass antibodies. [ABSTRACT FROM AUTHOR]

Published
1994

33. Characterization of Neisseria meningitidisStrains Causing Disease in Complement-Deficient and Complement-Sufficient Patients

Author

Fijen, C. A. P., Kuijper, E. J., Dankert, J., Daha, M. R., and Caugant, D. A.

Abstract

ABSTRACTSerotyping and serosubtyping of meningococci showed no difference between isolates from 44 complement-deficient persons and from 50 complement-sufficient persons with meningococcal disease. Multilocus enzyme electrophoretic typing of the meningococci revealed 54 electrophoretic types that were equally distributed among isolates from complement-deficient and complement-sufficient patients. Analysis of strains isolated from eight complement-deficient persons with 11 recurrences of meningococcal disease showed that one strain was identical to the strain previously isolated from the same individual. Our results indicate that there are no differences between the clonal distributions of strains infecting complement-deficient and complement-sufficient patients. Most recurrences were infections caused by different strains.

Published
1998
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36. [Haemophilus influenzae type a as the causative agent of meningitis in an infant].

Author

Mulder DC, Padberg RD, Westra M, and Fijen CA

Subjects
Amoxicillin therapeutic use, Anti-Bacterial Agents therapeutic use, Ceftriaxone therapeutic use, Female, Haemophilus Vaccines immunology, Haemophilus influenzae classification, Haemophilus influenzae immunology, Haemophilus influenzae type b immunology, Humans, Infant, Meningitis, Haemophilus drug therapy, Meningitis, Haemophilus prevention & control, Netherlands, Haemophilus influenzae pathogenicity, Meningitis, Haemophilus microbiology
Abstract

A 6-month-old girl had been ill with a cold for several days and was increasingly drowsy. She had been fully vaccinated against Haemophilus influenzae type b and had meningitis due to H. influenzae type a. She made a complete recovery after treatment with ceftriaxone and amoxicillin. In the Netherlands, vaccination with the conjugated H. influenzae type b vaccine was started in 1993 and since then invasive infections caused by H. influenzae type b have almost disappeared. Vaccination may suppress carriership of H. influenzae type b. However, vaccination does not elicit cross-protective antibodies against other serotypes of H. influenzae. H. influenzae non-type b may profit from the vaccination state, resulting in a higher carrier rate and an increased incidence of invasive infections. In the Netherlands, H. influenzae type a as the causative agent of an invasive infection has been recorded for the first time since registration started in 1975 and since then five such cases have been reported. In the literature, 45 cases of infection with H. influenzae type a have been described up until now.

Published
2002

38. Molecular characterisation of 10 Dutch properdin type I deficient families: mutation analysis and X-inactivation studies.

Author

van den Bogaard R, Fijen CA, Schipper MG, de Galan L, Kuijper EJ, and Mannens MM

Subjects
DNA analysis, DNA blood, DNA Mutational Analysis, Exons, Female, Humans, Lymphocytes physiology, Male, Netherlands, Pedigree, Polymerase Chain Reaction, Polymorphism, Genetic, Polymorphism, Single-Stranded Conformational, Properdin metabolism, X Chromosome genetics, Dosage Compensation, Genetic, Meningitis, Meningococcal genetics, Mutation, Missense, Properdin deficiency, Properdin genetics
Abstract

Properdin type I deficiency is characterised by complete absence of extracellular properdin, a positive regulator of the alternative pathway of complement activation. Properdin deficiency is associated with increased susceptibility to severe meningococcal disease. We have identified the genetic defect in 10 Dutch families. Six different mutations and one sequence polymorphism in the properdin gene were found. All amino acid substitutions were limited to conserved amino acids in exons 7 and 8 in contrast to the premature stops that were found in other exons. The missense mutations may alter the protein conformation in such a way that properdin will not be secreted and therefore catabolised intracellularly. The decreased properdin levels found in some healthy females carrying one mutated properdin gene were studied for X-inactivation. Most carriers with extreme low or high properdin levels showed preferential X-inactivation for the normal or mutated X chromosome, respectively. We observed some exceptions, suggesting additional regulation of properdin excretion apart from X-inactivation.

Published
2000
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39. Properdin deficiency: molecular basis and disease association.

Author

Fijen CA, van den Bogaard R, Schipper M, Mannens M, Schlesinger M, Nordin FG, Dankert J, Daha MR, Sjöholm AG, Truedsson L, and Kuijper EJ

Subjects
Amino Acid Sequence, Complement Pathway, Alternative, Humans, Meningococcal Infections genetics, Meningococcal Infections immunology, Molecular Sequence Data, Mutation, Phenotype, Repetitive Sequences, Amino Acid, Properdin deficiency, Properdin genetics
Published
1999
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40. Mannose-binding lectin and meningococcal disease.

Author

Kuijper EJ, Fijen CA, Dankert J, and Thiel S

Subjects
Alleles, Carrier Proteins blood, Collectins, Complement Activation, Gene Frequency, Humans, Mannans genetics, Meningococcal Infections blood, Meningococcal Infections immunology, Carrier Proteins genetics, Genetic Predisposition to Disease, Meningococcal Infections genetics
Published
1999
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41. [The bactericidal action of human neutrophils on meningococci in vitro].

Author

Platonov AE, Vershinina IV, Käyhty H, Fijen CA, and Kuijper EJ

Subjects
Bacterial Vaccines immunology, Complement System Proteins deficiency, Humans, Immunity, Cellular, Immunologic Deficiency Syndromes immunology, Meningococcal Infections immunology, Meningococcal Infections prevention & control, Time Factors, Vaccines, Combined immunology, Blood Bactericidal Activity immunology, Neisseria meningitidis immunology, Neutrophils immunology
Abstract

32 Russian patients with late complement component deficiency (LCCD) were immunize with tetravalent meningococcal polysaccharide vaccine (A + C + W135 + Y). Their immune response and infectious morbidity rate were followed for 6 years and the partial protective efficacy of vaccination was demonstrated. As the antibody-mediated complement-induced bactericidal activity of plasma was completely absent in persons with LCCD, the bactericidal action of human neutrophils on meningococci of groups A, W135 and B was studied under the conditions of incubation with serum samples collected from persons with LCCD before and after vaccination. In LCCD serum alone the exponential growth of meningococci was observed, while the addition of human neutrophils resulted in the essential inhibition of the growth of meningococci (up to their complete elimination). The proportion of serum samples stimulating the elimination of group A and W 135 meningococci by neutrophils was almost 40% of the serum samples collected before vaccination and significantly increased among the serum samples collected after vaccination (up to 84%) or revaccination (up to 90%). At the same time the capacity of an individual serum sample to promote the bactericidal effect of neutrophils against meningococci correlated with its content of specific anti-polysaccharide IgG and IgM antibodies, as well as antibodies to the inner core of lipopolysaccharide. The interaction of neutrophils with meningococci was significantly inhibited after incubation in heat-inactivated serum, suggesting that this interaction was partly mediated along the following path: the binding of IgM and IgG antibodies with bacteria--the activation of complement and the deposition of C3 complement on bacteria--the binding of meningococci with CR3 receptors of neutrophils.

Published
1999

42. Assessment of complement deficiency in patients with meningococcal disease in The Netherlands.

Author

Fijen CA, Kuijper EJ, te Bulte MT, Daha MR, and Dankert J

Subjects
Adolescent, Adult, Age Distribution, Cerebrospinal Fluid microbiology, Child, Child, Preschool, Humans, Infant, Newborn, Meningococcal Infections epidemiology, Meningococcal Infections genetics, Meningococcal Infections mortality, Middle Aged, Neisseria meningitidis classification, Neisseria meningitidis genetics, Netherlands epidemiology, Pedigree, Recurrence, Complement System Proteins deficiency, Meningococcal Infections immunology, Neisseria meningitidis immunology, Properdin deficiency
Abstract

The frequency of complement deficiency in 176 of 7,732 patients with meningococcal disease in the Netherlands from 1959 through 1992 was assessed. Complement deficiency was found in six patients (3%): 3 (7%) of the patients with Neisseria meningitidis serogroup C disease, 1 (2%) of the patients with N. meningitidis serogroup A disease, and 2 (33%) of the patients with infections due to uncommon serogroups and nongroupable strains of N. meningitidis. Of 91 additional patients with meningococcal infections due to uncommon serogroups, 33% also had complement deficiency. Thirty-four of the 36 complement-deficient patients with meningococcal disease who were from 33 families were 5 years of age or older. Twenty-six additional complement-deficient relatives were found. Screening individuals with meningococcal disease due to uncommon serogroups who were 5 years of age or older identified 30 of the 33 complement-deficient families. Only 27% of the complement-deficient relatives had had meningococcal disease. This risk was lower for relatives with properdin deficiency (18%) than for those deficient in the late component of complement (38%). Therefore, pedigree studies are warranted for identifying those complement-deficient persons who require vaccination for meningococcal disease.

Published
1999
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43. Human properdin deficiency has a heterogeneous genetic background.

Author

Truedsson L, Westberg J, Fredrikson GN, Sjöholm AG, Kuijper EJ, Fijen CA, Späth PJ, and Uhlén M

Subjects
Chromosome Mapping, Genetic Linkage, Humans, Male, Meningococcal Infections immunology, Phenotype, Properdin immunology, X Chromosome genetics, Meningococcal Infections genetics, Mutation genetics, Properdin deficiency, Properdin genetics
Published
1997
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44. The effect of mannan-binding lectin on opsonophagocytosis of Neisseria meningitidis.

Author

Drogari-Apiranthitou M, Fijen CA, Thiel S, Platonov A, Jensen L, Dankert J, and Kuijper EJ

Subjects
Bacterial Vaccines administration & dosage, Collectins, Colony-Forming Units Assay, Complement C1q immunology, Humans, Neisseria meningitidis immunology, Opsonin Proteins analysis, Phagocytosis immunology, Vaccination, Carrier Proteins pharmacology, Complement System Proteins deficiency, Lectins pharmacology, Mannans pharmacology, Neisseria meningitidis drug effects, Phagocytosis drug effects
Abstract

Mannan-binding lectin (MBL), an acute phase protein with a structure and a function very similar to that of C1q, is known to act as an opsonin binding to a number of microorganisms. In order to investigate the effect of MBL on the phagocytic killing of meningococci, a serogroup B meningococcal strain (H44/76) and its unencapsulated variant v24, as well as a serogroup A meningococcal strain were opsonized with MBL (purified from normal human plasma at the State Serum Institute, Denmark) and used in a phagocytic killing assay at a density of 7 x 10(3) CFU/ml. Polymorphonuclear cells (PMNs) from one healthy donor were isolated by density gradient centrifugation over Percoll and added to the system (7 x 10(6) cells/ml). In a first set of experiments without addition of serum or complement, no influence of MBL was observed on the killing of any of these strains. Addition of MBL to non-opsonized bacteria of the serogroup A strain did not result in enhanced killing either; on the contrary, the growth of this strain increased significantly when a high MBL concentration (40 micrograms/ml) was used in the presence of PMNs. Further investigations were performed using sera of five individuals with late complement component deficiency (LCCD) and a concomitant MBL deficiency, vaccinated with a tetra-valent (ACYW135) meningococcal capsular polysaccharide vaccine. Pre- and post-vaccination sera (50% final concentration) were tested against a group A strain opsonized or not with MBL. In only one patient was there a moderate increase of killing of the opsonized bacteria after vaccination compared to pre-vaccination serum. Our results suggest that MBL may not play a significant role in the opsonophagocytosis of meningococci, irrespective of its binding to unencapsulated and serogroup A strains.

Published
1997
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45. Comparison of commercial diagnostic tests for identification of serogroup antigens of Neisseria meningitidis.

Author

van der Ende A, Schuurman IG, Hopman CT, Fijen CA, and Dankert J

Subjects
Carrier State microbiology, Evaluation Studies as Topic, Humans, Meningitis, Meningococcal microbiology, Meningococcal Infections microbiology, Neisseria meningitidis isolation & purification, Sensitivity and Specificity, Serotyping statistics & numerical data, Antigens, Bacterial isolation & purification, Neisseria meningitidis classification, Neisseria meningitidis immunology, Serotyping methods
Abstract

In the study that is described the sensitivities and specificities of three commercial tests and the standard Reference Laboratory test, used since 1961, to identify Neisseria meningitidis serogroups were compared. The tests marketed by Difco, Murex/Wellcome, and Sanofi/Pasteur showed overall sensitivities of 92, 95, and 100%, respectively, and specificities of 67, 88, and 82%, respectively. When limited to the common serogroups A, B, and C, the three tests yielded sensitivities of 93, 97, and 100%, respectively, and specificities of 98, 100, and 98%, respectively. However, determination of the uncommon serogroups X, W-135, Y, Z, and 29E with these tests is either unreliable or not possible.

Published
1995
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46. C5 deficiency in a patient with primary Sjögren's syndrome.

Author

Schoonbrood TH, Hannema A, Fijen CA, Markusse HM, and Swaak AJ

Subjects
Adult, Complement Hemolytic Activity Assay, Female, Humans, Complement C5 deficiency, Sjogren's Syndrome blood
Abstract

We report a case of C5 deficiency in combination with Sjögren's syndrome (SS). Our patient presented with polyarthritis and complaints of oral and ocular dryness. In the serum there was a very low titer of total hemolytic complement (CH50) due to a deficiency of the fifth complement component. C5 deficiency is often associated with recurrent life threatening infections, membranous glomerulonephritis, and discoid lupus erythematosus, but it has not been described in association with primary SS.

Published
1995

47. Role of neutrophil Fc gamma RIIa (CD32) and Fc gamma RIIIb (CD16) polymorphic forms in phagocytosis of human IgG1- and IgG3-opsonized bacteria and erythrocytes.

Author

Bredius RG, Fijen CA, De Haas M, Kuijper EJ, Weening RS, Van de Winkel JG, and Out TA

Subjects
Bacteria immunology, Cells, Cultured, Erythrocytes immunology, Humans, Rho(D) Immune Globulin immunology, Rosette Formation, Antigens, CD, Immunoglobulin G immunology, Neutrophils immunology, Opsonin Proteins immunology, Phagocytosis immunology, Receptors, IgG immunology
Abstract

The four subclasses of IgG have different biological activities associated with their Fc regions. Fc gamma receptors on leucocytes (Fc gamma R) mediate binding and phagocytosis of opsonized particles. Two structurally and functionally distinct allelic polymorphisms of the Fc gamma R have been defined: the H/R131 forms of Fc gamma RIIa (CD32), and the neutrophil antigen 1 (NA1)/NA2 forms of Fc gamma RIIIb (CD16). In this study the activities of allotypes of CD16 are analysed with antibacterial IgG subclass antibodies and with IgG1 and IgG3 anti-Rhesus D, and the activities of CD32 with IgG1 and IgG3 anti-Rhesus D. With respect to the allotypes of CD16, polymorphonuclear leucocytes (PMN) homozygous for Fc gamma RIIb-NA2 exhibited a lower (21-25%) IgG1-mediated phagocytosis of Staphylococcus aureus strain Wood (STAW), Haemophilus influenzae type b (Hib), and Neisseria meningitidis group B (NMen) than IIIb-NA1 PMN. The difference was apparent only when the micro-organisms were opsonized in the absence of complement, and was furthermore enhanced (34-52%) upon blockade of Fc gamma RIIa. In addition, monoclonal IgG3 anti-D-mediated rosette formation and phagocytosis was consistently found to be lower (16%) with Fc gamma RIIIb-NA2 than with IIIb-NA1 PMN. For the allotypes of CD32 we now show that IgG3 anti-D sensitized erythrocytes formed more (50%) rosettes and were phagocytosed at a higher rate with PMN carrying Fc gamma RIIa-H131 than with PMN carrying IIa-R131. Heterozygous Fc gamma RIIa-H/R131 PMN exhibited intermediate phagocytic activity in this respect. This study illustrates a critical role of Fc gamma R allotypes in functional interactions with biologically relevant IgG subclass antibodies.

Published
1994

48. Deficiency of the beta subunit of the eighth component of complement presenting as arthritis and exanthem.

Author

Wulffraat NM, Sanders EA, Fijen CA, Hannema A, Kuis W, and Zegers BJ

Subjects
Adolescent, Adult, Arthritis, Juvenile immunology, Complement C8 genetics, Exanthema immunology, Family Health, Female, Heterozygote, Humans, Male, Middle Aged, Arthritis, Juvenile etiology, Complement C8 deficiency, Exanthema etiology
Abstract

A 13-year-old boy presented with juvenile chronic arthritis of 6 months' duration. Antinuclear antibodies, anti-double-stranded DNA antibodies, and rheumatoid factor were not detected. Western blotting showed a deficiency of the beta subunit of the eighth component of complement. The same deficiency was present in the patient's sister. C8 beta deficiency is usually detected in individuals who survive meningococcal disease. There was no such history in this family. Juvenile chronic arthritis has not previously been described in patients with C8 beta deficiency.

Published
1994
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49. Fc gamma receptor IIa (CD32) polymorphism in fulminant meningococcal septic shock in children.

Author

Bredius RG, Derkx BH, Fijen CA, de Wit TP, de Haas M, Weening RS, van de Winkel JG, and Out TA

Subjects
Adolescent, Child, Child, Preschool, Female, Humans, Immunoglobulin G blood, Immunoglobulin G classification, Infant, Male, Meningitis, Meningococcal genetics, Neutrophils immunology, Phagocytosis, Reference Values, Retrospective Studies, Shock, Septic genetics, White People genetics, Meningitis, Meningococcal immunology, Neisseria meningitidis immunology, Polymorphism, Genetic, Receptors, IgG genetics, Shock, Septic immunology
Abstract

Antibodies are essential in host defense against Neisseria meningitidis. Therefore, interactions among IgG and Fc receptors (Fc gamma R) on phagocytes may be crucial. Genetic polymorphic forms of Fc gamma RIIa (CD32) express different functional activities. In a retrospective study, Fc gamma R polymorphisms were determined in 25 children who survived fulminant meningococcal septic shock: 11 had Fc gamma RIIa-R/R131, the poor IgG2-binding allotype, which is a significantly more frequent rate than found in a healthy white population (44% vs. 23%; P = .028; odds ratio = 2.67; 95% confidence interval, 1.09-6.53). The relevance of this finding was further supported by the fact that neutrophils with the Fc gamma RIIa-R/R131 allotype phagocytized N. meningitidis opsonized with polyclonal IgG2 antibodies less effectively than did IIa-H/H131 neutrophils. Our findings suggest an important role for anti-N. meningitidis IgG2 and the Fc gamma RIIa polymorphism in host defense against systemic meningococcal infections.

Published
1994
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