Mapping and analysis of the lytic and fusogenic domains of surfactant protein B

Biochemistry

Volumn 44, Issue 3, 2005, Pages 861-872

  Ryan, Marnie A ^a   Qi, Xiaoyang ^a   Serrano, Alicia G ^b   Ikegami, Machiko ^a   Perez Gil, Jesus ^b   Johansson, Jan ^c   Weaver, Timothy E ^a  

^a UNIVERSITY OF CINCINNATI COLLEGE OF MEDICINE   (United States)

^b UNIVERSIDAD COMPLUTENSE DE MADRID   (Spain)

^c KAROLINSKA INSTITUTE   (Sweden)

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL ORGANS; CROSSLINKING; PHOSPHOLIPIDS; POLYPEPTIDES; PROTEINS; SUBSTITUTION REACTIONS; SURFACE ACTIVE AGENTS; SURFACE TENSION;

AMINO ACID PEPTIDES; MEMBRANE BINDING; SURFACTANT PROTEIN B (SP-B);

BIOCHEMISTRY;

AMINO ACID; DIPALMITOYLPHOSPHATIDYLCHOLINE; LIPOSOME; PHOSPHATIDYLGLYCEROL; PROTEIN; SURFACTANT; SURFACTANT PROTEIN B; SYNTHETIC PEPTIDE;

ADSORPTION; ALPHA HELIX; AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CROSS LINKING; FUSOGENIC DOMAIN; LYTIC DOMAIN; MEMBRANE BINDING; MEMBRANE FUSION; MEMBRANE PERMEABILITY; MEMBRANE STRUCTURE; PEPTIDE MAPPING; PHOSPHOLIPID MEMBRANE; PHOSPHOLIPID VESICLE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ANALYSIS; PROTEIN DOMAIN; PROTEIN INTERACTION; PROTEIN STRUCTURE; STRUCTURE ACTIVITY RELATION; SURFACE PROPERTY; SURFACE TENSION;

AMINO ACID SEQUENCE; HUMANS; LIPOSOMES; MOLECULAR SEQUENCE DATA; PULMONARY SURFACTANT-ASSOCIATED PROTEIN B; SEQUENCE HOMOLOGY, AMINO ACID; SURFACE TENSION;

EID: 12344310107     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0485575     Document Type: Article

References (47)

1. Clark, J. C., Wert, S. E., Bachurski, C. J., Stahlman, M. T., Stripp, B. R., Weaver, T. E., and Whitsett, J. A. (1995) Targeted disruption of the surfactant protein B gene disrupts surfactant homeostasis, causing respiratory failure in newborn mice, Proc. Natl. Acad. Sci. U.S.A. 92, 7794-7798.
2. Melton, K. R., Nesslein, L. L., Ikegami, M., Tichelaar, J. W., Clark, J. C., Whitsett, J. A., and Weaver, T. E. (2003) SP-B deficiency causes respiratory failure in adult mice, Am. J. Physiol. Lung Cell. Mol. Physiol. 285, L543-L549.
3. Patthy, L. (1991) Homology of the precursor of pulmonary surfactant-associated protein SP-B with prosaposin and sulfated glycoprotein-1, J. Biol. Chem. 266, 6035-6037.
4. Andersson, M., Curstedt, T., Jornvall, H., and Johansson, J. (1995) An amphipathic helical motif common to tumourolytic polypeptide NK-lysin and pulmonary surfactant polypeptide SP-B, FEBS Lett. 362, 328-332.
5. Baatz, J. E., Elledge, B., and Whitsett, J. A. (1990) Surfactant protein SP-B induces ordering at the surface of model membrane bilayers, Biochemistry 29, 6714-6720.
6. Vandenbussche, G., Clercx, A., Clercx, M., Curstedt, T., Johansson, J., Jornvall, H., and Ruysschaert, J. M. (1992) Secondary structure and orientation of the surfactant protein SP-B in a lipid environment-a Fourier transform infrared spectroscopy study, Biochemistry 31, 9169-9176.
7. Oosterlaken-Dijksterhuis, M. A., Van Eijk, M., Van Golde, L. M. G., and Haagsman, H. P. (1992) Lipid mixing is mediated by the hydrophobic surfactant protein SP-B but not by SP-C, Biochim. Biophys. Acta 1110, 45-50.
8. Poulain, F. R., Allen, L., Williams, M. C., Hamilton, R. L., and Hawgood, S. (1992) Effects of surfactant apolipoproteins on liposome structure-implications for tubular myelin formation, Am. J. Physiol. 262, L730-L739.
9. Shiffer, K., Hawgood, S., Duzgunes, N., and Goerke, J. (1988) Interactions of the low molecular weight group of surfactant-associated proteins (SP 5-18) with pulmonary surfactant lipids, Biochemistry 27, 2689-2695.
10. Vorbroker, D. K., Voorhout, W. F., Weaver, T. E., and Whitsett, J. A. (1995) Posttranslational processing of surfactant protein C in rat Type II cells, Am. J. Physiol. Lung Cell. Mol. Physiol. 269, L727-L733.
11. Voorhout, W. F., Veenendaal, T., Haagsman, H. P., Weaver, T. E., Whitsett, J. A., van Golde, L. M. G., and Geuze, H. J. (1992) Intracellular processing of pulmonary surfactant protein-B in an endosomal/lysosomal compartment, Am. J. Physiol. 263, L479-L486.
12. Conkright, J. J., Bridges, J. P., Na, C. L., Voorhout, W. F., Trapnell, B., Glasser, S. W., and Weaver, T. E. (2001) Secretion of surfactant protein C, an integral membrane protein, requires the N-terminal propeptide, J. Biol. Chem. 276, 14658-14664.
13. Brasch, F., Ochs, M., Kähne, T., Guttentag, S., Schauer-Vukasinovic, V., Derrick, M., Johnen, G., Kapp, N., Müller, K.-M., Richter, J., Giller, T., Hawgood, S., and Bühling, F. (2003) Involvement of napsin A in the C- and N-terminal processing of surfactant protein B in type 11 pneumocytes of the human lung, J. Biol. Chem. 278, 49006-49014.
14. Ueno, T., Linder, S., Na, C. L., Rice, W. R., Johansson, J., and Weaver, T. E. (2004) Processing of pulmonary surfactant protein B by napsin and cathepsin H, J. Biol. Chem. 279, 16178-16184.
15. Weaver, T. E., and Conkright, J. J. (2001) Function of surfactant proteins B and C, Annu. Rev. Physiol. 63, 555-578.
16. Nogee, L. M., Gamier, G., Dietz, H. C., Singer, L., Murphy, A. M., Demello, D. E., and Colten, H. R. (1994) A mutation in the surfactant protein B gene responsible for fatal neonatal respiratory disease in multiple kindreds, J. Clin. Invest. 93, 1860-1863.
17. Vorbroker, D. K., Profitt, S. A., Nogee, L. M., and Whitsett, J. A. (1995) Aberrant processing of surfactant protein C (SP-C) in hereditary SP-B deficiency, Am. J. Physiol. Lung Cell. Mol. Physiol. 268, L647-L656.
18. Stahlman, M. T., Gray, M. P., Falconieri, M. W., Whitsett, J. A., and Weaver, T. E. (2000) Lamellar body formation in normal and surfactant protein B-deficient fetal mice, Lab. Invest. 80, 395-403.
19. Weibel, E. R., and Gil, J. (1968) Electron microscopic demonstration of an extracellular duplex lining layer of alveoli, Respir. Physiol. 4, 42-57.
20. Perez-Gil, J., and Keough, K. M. (1998) Interfacial properties of surfactant proteins, Biochim. Biophys. Acta 1408, 203-217.
21. Suzuki, Y., Fujita, Y., and Kogishi, K. (1989) Reconstitution of tubular myelin from synthetic lipids and proteins associated with pig pulmonary surfactant, Am. Rev. Respir. Dis. 140, 75-81.
22. deMello, D. E., Heyman, S., Phelps, D. S., Hamvas, A., Nogee, L., Cole, S., and Colten, H. R. (1994) Ultrastructure of lung in surfactant protein B deficiency, Am. J. Respir. Cell Mol. Biol. 11, 230-239.
23. Liepinsh, E., Andersson, M., Ruysschaert, J. M., and Otting, G. (1997) Saposin fold revealed by the NMR structure of NK-lysin, Nat. Struct. Biol. 4, 793-795.
24. Shen, H. Q., Duan, C. X., Li, Z. Y., and Suzuki, Y. (1997) Effects of proteinosis surfactant proteins on the viability of rat alveolar macrophages, Am. J. Respir. Crit. Care Med. 156, 1679-1687.
25. Horowitz, A. D., Elledge, B., Whitsett, J. A., and Baatz, J. E. (1992) Effects of lung surfactant proteolipid SP-C on the organization of model membrane lipids-a fluorescence study, Biochim. Biophys. Acta 1107, 44-54.
26. Wang, Y., Grabowski, G. A., and Qi, X. (2003) Phospholipid vesicle fusion induced by saposin C, Arch. Biochem. Biophys. 415, 43-53.
27. Schurch, S., Green, F. H., and Bachofen, H. (1998) Formation and structure of surface films: captive bubble surfactometry, Biochim. Biophys. Acta 1408, 180-202.
28. Perez-Gil, J., and Keough, K. M. (1991) Identical and similar amino acid sequences in the pulmonary surfactant proteins SP-B and SP-C and hemerythrin and myohemerythrin-an example of "biochemical Velcro"?, Biochem. Int. 25, 715-721.
29. Wimley, W. C., and White, S. H. (1996) Experimentally determined hydrophobicity scale for proteins at membrane interfaces, Nat. Struct. Biol. 3, 842-848.
30. Wang, Y., Rao, K. M., and Demchuk, E. (2003) Topographical organization of the N-terminal segment of lung pulmonary surfactant protein B (SP-B(1-25)) in phospholipid bilayers, Biochemistry 42, 4015-4027.
31. Cruz, A., Casals, C., Plasencia, I., Marsh, D., and PerezGil, J. (1998) Depth profiles of pulmonary surfactant protein B in phosphatidylcholine bilayers, studied by fluorescence and electron spin resonance spectroscopy, Biochemistry 37, 9488-9496.
32. Hsu, C. H., Wu, S. H., Chang, D. K., and Chen, C. P. (2002) Structural characterizations of fusion peptide analogs of influenza virus hemagglutinin-Implication of the necessity of a helix-hinge-helix motif in fusion activity, J. Biol. Chem. 277, 22725-22733.
33. Shai, Y. (1999) Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides, Biochim. Biophys. Acta 1462, 55-70.
34. Qi, X., and Grabowski, G. A. (2001) Differential membrane interactions of saposins A and C: implications for the functional specificity, J. Biol. Chem. 276, 27010-27017.
35. Veldhuizen, E. J. A., Waring, A. J., Walther, F. J., Batenburg, J. J., vanGolde, L. M. G., and Haagsman, H. P. (2000) Dimeric N-terminal segment of human surfactant protein B (DSP-B1-25) has enhanced surface properties compared to monomeric SP-B1-25, Biophys. J. 79, 377-384.
36. Zaltash, S., Palmblad, M., Curstedt, T., Johansson, J., and Persson, B. (2000) Pulmonary surfactant protein B: a structural model and a functional analogue, Biochim. Biophys. Acta 1466, 179-186.
37. Chander, A., Johnson, R. G., Reicherter, J., and Fisher, A. B. (1986) Lung lamellar bodies maintain an acidic internal pH, J. Biol. Chem. 261, 6126-6131.
38. Oosterlaken-Dijksterhuis, M. A., Van Eijk, M., Vanbuel, B. L. M., Van Golde, L. M. G., and Haagsman, H. P. (1991) Surfactant protein composition of lamellar bodies isolated from rat lung, Biochem. J. 274, 115-119.
39. Oh, D., Shin, S. Y., Lee, S., Kang, J. H., Kim, S. D., Ryu, P. D., Hahm, K. S., and Kim, Y. (2000) Role of the hinge region and the tryptophan residue in the synthetic antimicrobial peptides, cecropin A(1-8)-magainin 2(1-12) and its analogues, on their antibiotic activities and structures, Biochemistry 39, 11855-11864.
40. Anderson, D. H., Sawaya, M. R., Cascio, D., Ernst, W., Modlin, R., Krensky, A., and Eisenberg, D. (2003) Granulysin crystal structure and a structure-derived lytic mechanism, J. Mol. Biol. 325, 355-365.
41. Bruni, R., Taeusch, H. W., and Waring, A. J. (1991) Surfactant protein-B-lipid interactions of synthetic peptides representing the amino-terminal amphipathic domain, Proc. Natl. Acad. Sci. U.S.A. 88, 7451-7455.
42. 1H NMR study in methanol, Eur. J. Biochem. 173, 139-146.
43. 1H NMR experiments show that the 23-residue magainin antibiotic peptide is an alpha-helix in dodecylphosphocholine micelles, sodium dodecyl sulfate micelles, and trifluoroethanol/water solution, J. Biomol. NMR 9, 127-135.
44. Holak, T. A., Engstrom, A., Kraulis, P. J., Lindeberg, G., Bennich, H., Jones, T. A., Gronenborn, A. M., and Clore, G. M. (1988) The solution conformation of the antibacterial peptide cecropin A: a nuclear magnetic resonance and dynamical simulated annealing study, Biochemistry 27, 7620-7629.
45. Ikura, T., Go, N., and Inagaki, F. (1991) Refined structure of melittin bound to perdeuterated dodecylphosphocholine micelles as studied by 2D-NMR and distance geometry calculation, Proteins 9, 81-89.
46. Sipos, D., Andersson, M., and Ehrenberg, A. (1992) The structure of the mammalian antibacterial peptide cecropin P1 in solution, determined by proton-NMR, Eur. J. Biochem. 209, 163-169.
47. Bruni, R., HernandezJuviel, J. M., Tanoviceanu, R., and Walther, F. J. (1998) Synthetic mimics of surfactant proteins B and C: In vitro surface activity and effects on lung compliance in two animal models of surfactant deficiency, Mol. Genet. Metab. 63, 116-125.