Cloning, sequence analysis and confirmation of derived gene sequences for three epitope-mapped monoclonal antibodies against human phagocyte flavocytochrome b

Molecular Immunology

Volumn 44, Issue 4, 2007, Pages 625-637

  Taylor, Ross M ^a   Maaty, Walid S A ^a   Lord, Connie I ^a   Hamilton, Trinity ^a   Burritt, James B ^a   Bothner, Brian ^a   Jesaitis, Algirdas J ^a  

^a MONTANA STATE UNIVERSITY   (United States)

Author keywords

Antibodies; Cloning; Flavocytochrome b; Mass spectrometry; Sequence

Indexed keywords

EPITOPE; LACTATE DEHYDROGENASE (CYTOCHROME); MONOCLONAL ANTIBODY;

ACCURACY; AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; CLONING; DIGESTION; DNA SEQUENCE; ENERGY TRANSFER; EPITOPE MAPPING; GENE AMPLIFICATION; GENE SEQUENCE; GENETIC HETEROGENEITY; HEAVY CHAIN; HUMAN; HUMAN CELL; LIGHT CHAIN; LIQUID CHROMATOGRAPHY; MASS SPECTROMETRY; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; NUCLEOTIDE SEQUENCE; PHAGOCYTE; PREDICTION; PRIORITY JOURNAL; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; SEQUENCE ANALYSIS; STRUCTURE ANALYSIS; TWO DIMENSIONAL ELECTROPHORESIS; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; ANIMALS; ANTIBODIES, MONOCLONAL; ANTIBODY SPECIFICITY; BINDING SITES, ANTIBODY; CLONING, MOLECULAR; CYTOCHROME B GROUP; EPITOPE MAPPING; HUMANS; IMMUNOGLOBULIN VARIABLE REGION; MICE; MOLECULAR CONFORMATION; MOLECULAR SEQUENCE DATA; NADPH OXIDASE; PHAGOCYTES; PROTEIN SUBUNITS; SEQUENCE ANALYSIS;

EID: 33747862002     PISSN: 01615890     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molimm.2005.10.022     Document Type: Article

References (45)

1. Abo A., Boyhan A., West I., Thrasher A.J., and Segal A.W. Reconstitution of neutrophil NADPH oxidase activity in the cell-free system by four components: p67-phox, p47-phox, p21rac1, and cytochrome b-245. J. Biol. Chem. 267 (1992) 16767-16770
2. Al Lazikani B., Lesk A.M., and Chothia C. Standard conformations for the canonical structures of immunoglobulins. J. Mol. Biol. 273 (1997) 927-948
3. Aybay C., and Imir T. Development of a rapid, single-step procedure using protein G affinity chromatography to deplete fetal calf serum of its IgG and to isolate murine IgG1 monoclonal antibodies from supernatants of hybridoma cells. J. Immunol. Meth. 233 (2000) 77-81
4. Babior B.M. Phagocytes and oxidative stress. Am. J. Med. 109 (2000) 33-44
5. Bailey B.W., Mumey B., Hargrave P.A., Arendt A., Ernst O.P., Hofmann K.P., Callis P.R., Burritt J.B., Jesaitis A.J., and Dratz E.A. Constraints on the conformation of the cytoplasmic face of dark-adapted and light-excited rhodopsin inferred from antirhodopsin antibody imprints. Protein Sci. 12 (2003) 2453-2475
6. Baniulis D., Burritt J.B., Taylor R.M., Dinauer M.C., Heyworth P.G., Parkos C.A., Magnusson K.E., and Jesaitis A.J. Monoclonal antibody CL5 recognizes the amino terminal domain of human phagocyte flavocytochrome b558 large subunit, gp91phox. Eur. J. Haematol. 74 (2005) 337-347
7. Biberstine-Kinkade K.J., DeLeo F.R., Epstein R.I., LeRoy B.A., Nauseef W.M., and Dinauer M.C. Heme-ligating histidines in flavocytochrome b(558): identification of specific histidines in gp91(phox). J. Biol. Chem. 276 (2001) 31105-31112
8. Burritt J.B., Bond C.W., Doss K.W., and Jesaitis A.J. Filamentous phage display of oligopeptide libraries. Anal. Biochem. 238 (1996) 1-13
9. Burritt J.B., Busse S.C., Gizachew D., Siemsen D.W., Quinn M.T., Bond C.W., Dratz E.A., and Jesaitis A.J. Antibody imprint of a membrane protein surface. Phagocyte flavocytochrome b. J. Biol. Chem. 273 (1998) 24847-24852
10. Burritt J.B., DeLeo F.R., McDonald C.L., Prigge J.R., Dinauer M.C., Nakamura M., Nauseef W.M., and Jesaitis A.J. Phage display epitope mapping of human neutrophil flavocytochrome b558. Identification of two juxtaposed extracellular domains. J. Biol. Chem. 276 (2001) 2053-2061
11. Burritt J.B., Foubert T.R., Baniulis D., Lord C.I., Taylor R.M., Mills J.S., Baughan T.D., Roos D., Parkos C.A., and Jesaitis A.J. Functional epitope on human neutrophil flavocytochrome b558. J. Immunol. 170 (2003) 6082-6089
12. Burritt J.B., Quinn M.T., Jutila M.A., Bond C.W., and Jesaitis A.J. Topological mapping of neutrophil cytochrome b epitopes with phage-display libraries. J. Biol. Chem. 270 (1995) 16974-16980
13. Chardes T., Villard S., Ferrieres G., Piechaczyk M., Cerutti M., Devauchelle G., and Pau B. Efficient amplification and direct sequencing of mouse variable regions from any immunoglobulin gene family. FEBS Lett. 452 (1999) 386-394
14. Cheng G., Cao Z., Xu X., van Meir E.G., and Lambeth J.D. Homologs of gp91phox: cloning and tissue expression of Nox3, Nox4, and Nox5. Gene 269 (2001) 131-140
15. Cross A.R., Rae J., and Curnutte J.T. Cytochrome b-245 of the neutrophil superoxide-generating system contains two nonidentical hemes. Potentiometric studies of a mutant form of gp91phox. J. Biol. Chem. 270 (1995) 17075-17077
16. Cross A.R., and Segal A.W. The NADPH oxidase of professional phagocytes-prototype of the NOX electron transport chain systems. Biochim. Biophys. Acta 1657 (2004) 1-22
17. Dahan I., Issaeva I., Gorzalczany Y., Sigal N., Hirshberg M., and Pick E. Mapping of functional domains in the p22(phox) subunit of flavocytochrome b(559) participating in the assembly of the NADPH oxidase complex by "peptide walking". J. Biol. Chem. 277 (2002) 8421-8432
18. Davis A.R., Mascolo P.L., Bunger P.L., Sipes K.M., and Quinn M.T. Cloning and sequencing of the bovine flavocytochrome b subunit proteins, gp91-phox and p22-phox: comparison with other known flavocytochrome b sequences. J. Leukoc. Biol. 64 (1998) 114-123
19. de Haard H., Kazemier B., van der B.A., Oudshoorn P., Boender P., Arends J.W., and van Gemen B. Vernier zone residue 4 of mouse subgroup II kappa light chains is a critical determinant for antigen recognition. Immunotechnology 4 (1999) 203-215
20. de Haard H.J., Kazemier B., van der B.A., Oudshoorn P., Boender P., van Gemen B., Arends J.W., and Hoogenboom H.R. Absolute conservation of residue 6 of immunoglobulin heavy chain variable regions of class IIA is required for correct folding. Protein Eng. 11 (1998) 1267-1276
21. DeLeo F.R., Burritt J.B., Yu L., Jesaitis A.J., Dinauer M.C., and Nauseef W.M. Processing and maturation of flavocytochrome b558 include incorporation of heme as a prerequisite for heterodimer assembly. J. Biol. Chem. 275 (2000) 13986-13993
22. Doussiere J., Brandolin G., Derrien V., and Vignais P.V. Critical assessment of the presence of an NADPH binding site on neutrophil cytochrome b558 by photoaffinity and immunochemical labeling. Biochemistry 32 (1993) 8880-8887
23. 2(-)-generating oxidase of neutrophils by an azido derivative of FAD. Biochemistry 34 (1995) 1760-1770
24. Geiszt M., and Leto T.L. The Nox family of NAD(P)H oxidases: host defense and beyond. J. Biol. Chem. 279 (2004) 51715-51718
25. Hampton M.B., Kettle A.J., and Winterbourn C.C. Inside the neutrophil phagosome: oxidants, myeloperoxidase, and bacterial killing. Blood 92 (1998) 3007-3017
26. Koshkin V., and Pick E. Generation of superoxide by purified and relipidated cytochrome b559 in the absence of cytosolic activators. FEBS Lett. 327 (1993) 57-62
27. Krebber A., Bornhauser S., Burmester J., Honegger A., Willuda J., Bosshard H.R., and Pluckthun A. Reliable cloning of functional antibody variable domains from hybridomas and spleen cell repertoires employing a reengineered phage display system. J. Immunol. Meth. 201 (1997) 35-55
28. Lambeth J.D. NOX enzymes and the biology of reactive oxygen. Nat. Rev. Immunol. 4 (2004) 181-189
29. Lan F., Umeda M., and Inoue K. Extended fitness of variable region primers by a novel PCR protocol. J. Immunol. Meth. 195 (1996) 27-32
30. Mates J.M., Perez-Gomez C., and Nunez D.C.I. Antioxidant enzymes and human diseases. Clin. Biochem. 32 (1999) 595-603
31. McCord J.M. The evolution of free radicals and oxidative stress. Am. J. Med. 108 (2000) 652-659
32. Morea V., Tramontano A., Rustici M., Chothia C., and Lesk A.M. Conformations of the third hypervariable region in the VH domain of immunoglobulins. J. Mol. Biol. 275 (1998) 269-294
33. Mortz E., Krogh T.N., Vorum H., and Gorg A. Improved silver staining protocols for high sensitivity protein identification using matrix-assisted laser desorption/ionization-time of flight analysis. Proteomics 1 (2001) 1359-1363
34. Mumey B.M., Bailey B.W., Kirkpatrick B., Jesaitis A.J., Angel T., and Dratz E.A. A new method for mapping discontinuous antibody epitopes to reveal structural features of proteins. J. Comput. Biol. 10 (2003) 555-567
35. Nisimoto Y., Otsuka-Murakami H., and Lambeth D.J. Reconstitution of flavin-depleted neutrophil flavocytochrome b558 with 8-mercapto-FAD and characterization of the flavin-reconstituted enzyme. J. Biol. Chem. 270 (1995) 16428-16434
36. Orum H., Andersen P.S., Oster A., Johansen L.K., Riise E., Bjornvad M., Svendsen I., and Engberg J. Efficient method for constructing comprehensive murine Fab antibody libraries displayed on phage. Nucl. Acids Res. 21 (1993) 4491-4498
37. Parkos C.A., Allen R.A., Cochrane C.G., and Jesaitis A.J. Purified cytochrome b from human granulocyte plasma membrane is comprised of two polypeptides with relative molecular weights of 91,000 and 22,000. J. Clin. Invest. 80 (1987) 732-742
38. Parkos C.A., Dinauer M.C., Jesaitis A.J., Orkin S.H., and Curnutte J.T. Absence of both the 91 and 22 kD subunits of human neutrophil cytochrome b in two genetic forms of chronic granulomatous disease. Blood 73 (1989) 1416-1420
39. Quinn M.T., Evans T., Loetterle L.R., Jesaitis A.J., and Bokoch G.M. Translocation of Rac correlates with NADPH oxidase activation. Evidence for equimolar translocation of oxidase components. J. Biol. Chem. 268 (1993) 20983-20987
40. Taylor R.M., Burritt J.B., Baniulis D., Foubert T.R., Lord C.I., Dinauer M.C., Parkos C.A., and Jesaitis A.J. Site-specific inhibitors of NADPH oxidase activity and structural probes of flavocytochrome b: characterization of six monoclonal antibodies to the p22phox subunit. J. Immunol. 173 (2004) 7349-7357
41. Taylor R.M., Burritt J.B., Foubert T.R., Snodgrass M.A., Stone K.C., Baniulis D., Gripentrog J.M., Lord C., and Jesaitis A.J. Single-step immunoaffinity purification and characterization of dodecylmaltoside-solubilized human neutrophil flavocytochrome b. Biochim. Biophys. Acta 1612 (2003) 65-75
42. Taylor R.M., Foubert T.R., Burritt J.B., Baniulis D., McPhail L.C., and Jesaitis A.J. Anionic amphiphile and phospholipid-induced conformational changes in human neutrophil flavocytochrome b observed by fluorescence resonance energy transfer. Biochim. Biophys. Acta 1663 (2004) 201-213
43. Vignais P.V. The superoxide-generating NADPH oxidase: structural aspects and activation mechanism. Cell Mol. Life Sci. 59 (2002) 1428-1459
44. Wang Z., Raifu M., Howard M., Smith L., Hansen D., Goldsby R., and Ratner D. Universal PCR amplification of mouse immunoglobulin gene variable regions: the design of degenerate primers and an assessment of the effect of DNA polymerase 3′ to 5′ exonuclease activity. J. Immunol. Meth. 233 (2000) 167-177
45. Yuan X., Gubbins M.J., and Berry J.D. A simple and rapid protocol for the sequence determination of functional kappa light chain cDNAs from aberrant-chain-positive murine hybridomas. J. Immunol. Meth. 294 (2004) 199-207