Relevant bibliographies by topics / Protein-Surfactant

Contents

  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'Protein-Surfactant'

Author: Grafiati
Published: 7 September 2023

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Journal articles on the topic "Protein-Surfactant"

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La Mesa, Camillo. "Polymer–surfactant and protein–surfactant interactions." Journal of Colloid and Interface Science 286, no. 1 (June 2005): 148–57. http://dx.doi.org/10.1016/j.jcis.2004.12.038.

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Thompson, Mark W. "Surfactant Protein B Deficiency: Insights into Surfactant Function through Clinical Surfactant Protein Deficiency." American Journal of the Medical Sciences 321, no. 1 (January 2001): 26–32. http://dx.doi.org/10.1097/00000441-200101000-00005.

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Wright, Jo Rae, Paul Borron, Karen G. Brinker, and Rodney J. Folz. "Surfactant Protein A." American Journal of Respiratory Cell and Molecular Biology 24, no. 5 (May 2001): 513–17. http://dx.doi.org/10.1165/ajrcmb.24.5.f208.

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CASALS, Cristina, Miguel L. F. RUANO, Eugenio MIGUEL, Paloma SANCHEZ, and Jesus PEREZ-GIL. "SURFACTANT PROTEIN-C ENHANCES LIPID AGGREGATION ACTIVITY OF SURFACTANT PROTEIN-A." Biochemical Society Transactions 22, no. 3 (August 1, 1994): 370S. http://dx.doi.org/10.1042/bst022370s.

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Mason, Robert J., Kelly Greene, and Dennis R. Voelker. "Surfactant protein A and surfactant protein D in health and disease." American Journal of Physiology-Lung Cellular and Molecular Physiology 275, no. 1 (July 1, 1998): L1—L13. http://dx.doi.org/10.1152/ajplung.1998.275.1.l1.

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Surfactant protein (SP) A and SP-D are collagenous glycoproteins with multiple functions in the lung. Both of these proteins are calcium-dependent lectins and are structurally similar to mannose-binding protein and bovine conglutinin. Both form polyvalent multimeric structures for interactions with pathogens, cells, or other molecules. SP-A is an integral part of the surfactant system, binds phospholipids avidly, and is found in lamellar bodies and tubular myelin. Initially, most research interest focused on its role in surfactant homeostasis. Recently, more attention has been placed on the role of SP-A as a host defense molecule and its interactions with pathogens and phagocytic cells. SP-D is much less involved with the surfactant system. SP-D appears to be primarily a host defense molecule that binds surfactant phospholipids poorly and is not found in lamellar inclusion bodies or tubular myelin. Both SP-A and SP-D bind a wide spectrum of pathogens including viruses, bacteria, fungi, and pneumocystis. In addition, both molecules have been measured in the systemic circulation by immunologic methods and may be useful biomarkers of disease. The current challenges are characterization of the three-dimensional crystal structure of SP-A and SP-D, molecular cloning of their receptors, and determination of their precise physiological functions in vivo.
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Sorensen, Grith Lykke, Steffen Husby, and Uffe Holmskov. "Surfactant protein A and surfactant protein D variation in pulmonary disease." Immunobiology 212, no. 4-5 (June 2007): 381–416. http://dx.doi.org/10.1016/j.imbio.2007.01.003.

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Ikegami, M., T. R. Korfhagen, M. D. Bruno, J. A. Whitsett, and A. H. Jobe. "Surfactant metabolism in surfactant protein A-deficient mice." American Journal of Physiology-Lung Cellular and Molecular Physiology 272, no. 3 (March 1, 1997): L479—L485. http://dx.doi.org/10.1152/ajplung.1997.272.3.l479.

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In the present study we asked if surfactant metabolism was altered in surfactant protein (SP) A-deficient mice in vivo. Although previous studies in vitro demonstrated that SP-A modulates surfactant secretion and reuptake by type II cells, mice made SP-A deficient by homologous recombination grow and reproduce normally and have normal lung function. Alveolar and lung tissue saturated phophatidylcholine (Sat PC) pools were 50 and 26% larger, respectively, in SP-A(-/-) mice than in SP-A(+/+) mice. Radiolabeled choline and palmitate incorporation into lung Sat PC was similar both in vivo and for lung tissue slices in vitro from SP-A(+/+) and SP-A(-/-) mice. Percent secretion of radiolabeled Sat PC was unchanged from 3 to 15 h, although SP-A(-/-) mice retained more labeled Sat PC in the alveolar lavages at 48 h (consistent with the increased surfactant pool sizes). Clearance of radiolabeled dipalmitoylphosphatidylcholine and SP-B from the air spaces after intratracheal injection was similar in SP-A(-/-) and SP-A(+/+) mice. Lack of SP-A had minimal effects on the overall metabolism of Sat PC or SP-B in mice.
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Korfhagen, Thomas R., Vladimir Sheftelyevich, Michael S. Burhans, Michael D. Bruno, Gary F. Ross, Susan E. Wert, Mildred T. Stahlman, et al. "Surfactant Protein-D Regulates Surfactant Phospholipid Homeostasisin Vivo." Journal of Biological Chemistry 273, no. 43 (October 23, 1998): 28438–43. http://dx.doi.org/10.1074/jbc.273.43.28438.

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Fulton, Barbara K., and Mary M. Davis. "SURFACTANT PROTEIN B DEFICIENCY." Pediatric Pathology & Molecular Medicine 21, no. 5 (January 2002): 507–11. http://dx.doi.org/10.1080/pdp.21.5.507.511.

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De Pasquale, Carmine G., Leonard F. Arnolda, Ian R. Doyle, Philip E. Aylward, Derek P. Chew, and Andrew D. Bersten. "Plasma Surfactant Protein-B." Circulation 110, no. 9 (August 31, 2004): 1091–96. http://dx.doi.org/10.1161/01.cir.0000140260.73611.fa.

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Dissertations / Theses on the topic "Protein-Surfactant"

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Valstar, Ank. "Protein-surfactant interactions." Doctoral thesis, Uppsala University, Department of Physical Chemistry, 2000. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-1070.

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Protein-surfactant interactions in aqueous media have been investigated. The globular proteins lysozyme and bovine serum albumin (BSA) served as model proteins. Several ionic and non-ionic surfactants were used.

Fluorescence probe measurements showed that at low sodium dodecyl sulfate (SDS) concentration (< 0.1 M) one micelle-like SDS cluster is bound to lysozyme. From dynamic light scattering (DLS) results it was observed that lysozyme in the complex does not correspond to the fully unfolded protein. At high SDS concentration (> 0.1 M) one compact and one more extended lysozyme-SDS complex coexist.

The influence of surfactant alkyl chain length and headgroup on BSA-surfactant complex formation was investigated. In these studies, binding isotherms were determined by nuclear magnetic resonance (NMR), DLS was used to measure the hydrodynamic radii of the complexes and the size of the micelle-like aggregates on BSA was determined using fluorescence probe methods.

It was observed from fluorescence measurements that the number of bound SDS molecules does not depend on the presence of the disulfide bridges. Reduced proteins wrap more efficiently around the micelle-like structures, resulting in somewhat smaller complexes, as observed with DLS.

Concentrated BSA-SDS solutions and the corresponding heat-set gels were investigated using DLS and fluorescence probe methods. Correlation lengths in the gel were determined and it was concluded that SDS forms micelle-like aggregates on BSA in concentrated solution and gel phase. The gel region in the ternary phase diagram BSA-SDS-3.1 mM NaN3 has been determined at room temperature.

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Cheng, Shu Ian. "Protein separation using surfactant precipitation." Thesis, Imperial College London, 2012. http://hdl.handle.net/10044/1/9282.

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Surfactant precipitation applied as a surfactant mediated protein purification technique has considerable potential in protein extraction, and therefore the understanding of the interactions involved and the folding behaviour in the precipitated protein was the first aim of this thesis. The key system parameters such as buffer salt concentration, molar ratio of surfactant to protein and pH which determines the protein stability in protein-surfactant complex formation were evaluated. The surfactant:protein ratio determines saturation of protein binding sites while pH determines the strength of affinity for ionic binding which influences hydrophobic binding with surfactant monomers causing the protein to lose its conformation. The protein-surfactant binding varied for lysozyme, cytochrome c and ribonuclease A with trypsin and α -chymotrypsin, and hence the denaturation profile. In the second aim, protein recovery from surfactant precipitation was enhanced by improving the solvent recovery method and, implementing a new and novel counterionic surfactant recovery method. The effect of a variety of recovery phases and solution conditions on lysozyme recovery was analysed in terms of their ability in maintaining protein stability, recovery yield, and activity. It was found that solvent recovery was limited by solvent polarity and protein solubility, and that the cationic surfactant, trioctylmethylammonium chloride (TOMAC), used to form nonpolar ion pairs with sodium bis-(2-ethylhexyl) sulfosuccinate (AOT) was the most efficient method for recovering protein. The third aim was to assess the influence of protein properties, such as charge and hydrophobicity, on protein separation. The selective extraction of a target protein from mixtures of proteins in both buffer and fermentation broth was investigated. It appears that the optimum surfactant:protein molar ratio for the extraction of the proteins from fermentation broth (lysozyme, cytochrome c and ribonuclease A; 16, 17 and 22 respectively) were similar to those in a buffer system. Lysozyme and ribonuclease A were selectively separated from a binary mixture. The extraction behaviour was well represented by surface charge distribution which is indifferent to system conditions. However, certain broth constituents induced the formation of some unfolded irreversible non-dissolvable precipitate in the recovery process. Finally, the use of non-ionic surfactants, ionic/non-ionic mixed surfactants, and cationic surfactants were investigated in surfactant precipitation system. Non-ionic surfactant does not support direct precipitation of proteins using surfactant or recovery of protein from a protein-surfactant complex, and has no effect in a mixed ionic/non-ionic system. The application of cationic surfactant precipitation to separate trypsin inhibitor was attempted, and good recovery was obtained.
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Faizal, Wong Fadzlie Wong. "Protein separation using surfactant precipitation." Thesis, Imperial College London, 2015. http://hdl.handle.net/10044/1/46041.

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Protein precipitation using a variety of surfactants has been shown to have considerable potential as a protein separation technique, and considerable work on using anionic surfactants has been carried out by previous researchers. However, anionic surfactants are only suitable for high pI proteins due to concerns about protein stability. Therefore, the first aim of this work was to develop a surfactant precipitation method for low pI proteins based on using cationic surfactants. The effect of important parameters such as the molar ratio of TOMAC to protein (Rp), and pH on the precipitation of bovine serum albumin, α-amylase, and trypsin inhibitor were examined. Recovery of the TOMAC-protein complex by solvent extraction and counter-ionic surfactant (AOT) was also studied. Varied results were obtained for the three proteins, and were correlated with protein properties, and it was found that the protein’s hydrophobicity and molecular weight were the best predictors for precipitation efficiency and recovery. The second aim of this research was to examine the feasibility of using a biocompatible surfactant – methyl ester sulphonate (MES) as a precipitating-ligand for target proteins in this surfactant precipitation technique. This work was a major breakthrough in the application of a new generation of ‘green’ surfactants for protein extraction. Lysozyme was used as a model protein in a single component system, and the influence of Rp, and pH were examined. Similarly, the recovery of the precipitate using solvent extraction and a counter-ionic surfactant, AOT, was studied. The performance of MES in precipitation was compared to a conventional surfactant, AOT, and it was found that their performance was comparable. This further highlighted its potential to be used as precipitant in protein purification. The third aim of this work was to apply the surfactant precipitation method to the purification of a target protein from a real industrial sample. Bacteriocin produced by Pediococcus acidilactici Kp10 was chosen as a target protein for this purpose. With a concentration of 11.56 mM of AOT (pH 4), precipitate recovery by acetone (0.99 mM NaCl), and a final recovery phase of 20 mM PBS (pH 7), about 86.3% of overall activity recovery, and a purification factor of about 53.8 was obtained. Further, this separation technique was shown to be better than reverse micellar extraction, and aqueous two-phase extraction in terms of performance. Hence, the surfactant precipitation technique was proven to be an effective and a viable separation method.
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Gomez, Gil Leticia. "The interaction between cholesterol and surfactant protein-c in lung surfactant." Doctoral thesis, Universite Libre de Bruxelles, 2009. http://hdl.handle.net/2013/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/210205.

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The presence of cholesterol is critical in defining a dynamic lateral structure in pulmonary

surfactant membranes, including the segregation of fluid-ordered and fluid-disordered phases.

However, an excess of cholesterol has been associated with impaired surface activity both in

surfactant models and in surfactant from injured lungs. It has also been reported that surfactant

protein SP-C interacts with cholesterol in lipid/protein interfacial films. In the present study, we

have analyzed the effect of SP-C on the thermodynamic properties of phospholipid membranes

containing cholesterol and on the ability of lipid/protein complexes containing surfactant

proteins and cholesterol to form and re-spread interfacial films capable of producing very low

surface tensions upon repetitive compression-expansion cycling. We have also analyzed the effect of cholesterol on the

structure, orientation and dynamic properties of SP-C embedded in physiologically relevant

model membranes.


Doctorat en Sciences
info:eu-repo/semantics/nonPublished

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Wiesener, Annegret. "Proteolytische Degradation von Surfactant Protein D." Diss., lmu, 2002. http://nbn-resolving.de/urn:nbn:de:bvb:19-6462.

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Yixiong, Zhang. "Functional protein-polymer surfactant hybrid nanomaterials." Thesis, University of Bristol, 2014. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.680356.

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This thesis presents the investigation of protein-polymer surfactant hybrid nanoconstructs prepared through the surface modification of haemoglobin (Hb) or glucose oxidase (GOx). These discrete stoichiometric conjugates of protein and polymer (with respect to charge) exhibited liquid-like behaviour close to room temperature in absence of solvents. Solvent-free Hb nanoconstructs could be readily dispersed into various organic solvents to form stable molecular protein-polymer surfactant conjugates. Spectroscopic studies showed that surface modification effectively protected the secondary structures of Hb from denaturing under non-aqueous conditions. Importantly, Hb-polymer surfactant conjugates displayed significantly enhanced peroxidase activity in organic solvents compared to their native counterparts, suggesting the polymer surfactant corona successfully shielded the enzyme-bound water layer and increased the protein's functional dynamics for non-aqueous catalysis. Solvent-free GOx nanoconstructs showed unprecedented phase behaviour because of the shape anisotropy of the protein. Below the melting point (40°C), the nanoconstructs exhibited spherulitic mesolamellar structures with an interlayer distance of "'12 nm due to the polyethylene glycol (PEG) chain-chain and alkyl tail-tail interactions within the polymer surfactants of the nanoconjugates. Upon melting, the spherulites transformed into a solvent-free liquid which displayed another PEG-mediated anisotropic phase with dendritic morphology that persisted until the conformation transition temperature (Te) of GOx (58°C). This suggested that the change in intra-polypeptide motions of the protein core during Te significantly influenced the intermolecular interactions of the solvents-free GOx-polymer nanoconjugates. With retained enzymatic activity, GOx-polymer surfactant nanoconjugates were effectively immobilized onto a porous membrane to serve as reusable biocatalysts. The resultant fabricated enzyme-based membrane exhibited greatly improved catalytic efficiency for oxidation of D-glucose. Moreover, incorporation of this enzyme membrane into a glucose-based hydrogel provided a constant release of oxygen (in the form of hydrogen peroxide) over a long period of time, which could offer new opportunities in the development of dressing for wound healing.
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Kamalanathan, Ishara Dedunu. "Foam fractionation of surfactant-protein mixtures." Thesis, University of Manchester, 2015. https://www.research.manchester.ac.uk/portal/en/theses/foam-fractionation-of-surfactantprotein-mixtures(a6484b1a-d796-45ff-bc5c-420ef9130363).html.

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Foam fractionation is an adsorptive bubble separation technology that has shown potential as a replacement to the more costly and non-sustainable traditional downstream processing methods such as solvent extraction and chromatography for biological systems. However biological systems mostly tend to be a mixture of surface active species that complicates the foam fractionation separation. In this thesis a detailed experimental study on the application of foam fractionation to separate a well-defined surfactant-protein mixture was performed with emphasis on the competitive adsorption behaviour and transport processes of surfactant-protein mixtures in a foam fractionation process. Surface tension and nuclear magnetic resonance (NMR) measurements showed that nonionic surfactant Triton X−100 maximum surface pressure, surface affinity and diffusivity were a factor of 2.05, 67.0 and 19.6 respectively greater than that of BSA. Thus Triton X−100 dominated the surface adsorption at an air-water surface by diffusing to the surface and adsorbing at the surface faster than BSA. This competitive adsorption behaviour was observed in foam fractionation experiments performed for Triton X−100/BSA mixtures for different feed concentration ratios and air flow rates. The recovery and enrichment of Triton X−100 were found to increase and decrease respectively with increasing air flow rate for all foam fractionation experiments as expected for a single component system. However the recovery and enrichment of BSA were both found to increase with increasing air flow rate for high feed concentrations of Triton X−100.Bubble size measurements of the foamate produced from foam fractionation experiments showed that at steady state conditions the bubbles rising from the liquid pool were stabilised by BSA. However at the top of the column the recovery of Triton X−100 in the foamate (75% to 100%) was always greater than the recovery of BSA (13% to 76%) for all foam fractionation experiments. In addition, for high feed concentrations of both components and at low air flow rates, the enrichment of BSA remained at almost unity for most experiments and only increased when the recovery of Triton X−100 reached 100%. Thus it was concluded that Triton X-100 displaced the adsorbed BSA from the surface. The foam drainage properties of Triton X−100/BSA mixtures were characterised using two methods; forced foam drainage and from pressure profiles of steady state foam fractionation experiments (pressure method). The drainage data from the forced foam drainage was found not to be compatible with experimental foam fractionation results, by indicating that stable foam was not produced during the foam fractionation experiments. However stable foam was repeatedly produced during foam fractionation experiments. The drainage data from the pressure method was found to be in close agreement to experimental foam fractionation experiments. The work in this thesis takes a significant step beyond the literature experimental foam fractionation studies for multicomponent systems. In addition to investigating the effect of foam fractionation process parameters on the separation of mixed systems, the results from the characterisation studies of surface adsorption and foam properties provided insight and deeper understanding of the competitive adsorption behaviour of surfactants and proteins in a foam fractionation process.
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Worthman, Lynn-Ann D. "Surfactant protein A (SP-A) affects pulmonary surfactant morphology and biophysical properties." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1997. http://www.collectionscanada.ca/obj/s4/f2/dsk2/tape16/PQDD_0014/MQ34241.pdf.

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Schiefelbein, Lars. "Sugar-Based Surfactant for Pharmaceutical Protein Formulations." Diss., lmu, 2011. http://nbn-resolving.de/urn:nbn:de:bvb:19-132870.

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Johnson, Conkright Juliana j. "SORTING AND SECRETION OF SURFACTANT PROTEIN C." University of Cincinnati / OhioLINK, 2001. http://rave.ohiolink.edu/etdc/view?acc_num=ucin990723467.

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Books on the topic "Protein-Surfactant"

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Verfasser, Schließmann Stephan J., Kirschbaum Andreas Verfasser, Plönes Till 1976 Verfasser, Müller-Quernheim Joachim 1953 Verfasser, Zissel Gernot Verfasser, Klinik für Pneumologie, Albert-Ludwigs-Universität Freiburg Medizinische Fakultät, and Albert-Ludwigs-Universität Freiburg, eds. Roflumilast-N-oxide induces surfactant protein expression in human alveolar epithelial cells type II. Freiburg: Universität, 2012.

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Xia, Jiding. Protein-Based Surfactants: Synthesis: Physicochemical Properties, and Applications (Surfactant Science). CRC, 2001.

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Book chapters on the topic "Protein-Surfactant"

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Randolph, Theodore W., and LaToya S. Jones. "Surfactant-Protein Interactions." In Pharmaceutical Biotechnology, 159–75. Boston, MA: Springer US, 2002. http://dx.doi.org/10.1007/978-1-4615-0557-0_7.

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Gupta, Rajesh K., and Anita Gupta. "Surfactant Protein-D." In Animal Lectins: Form, Function and Clinical Applications, 527–50. Vienna: Springer Vienna, 2012. http://dx.doi.org/10.1007/978-3-7091-1065-2_25.

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Jones, LaToya S., Narendra B. Bam, and Theodore W. Randolph. "Surfactant-Stabilized Protein Formulations: A Review of Protein-Surfactant Interactions and Novel Analytical Methodologies." In ACS Symposium Series, 206–22. Washington, DC: American Chemical Society, 1997. http://dx.doi.org/10.1021/bk-1997-0675.ch012.

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Arnebrant, Thomas, and Marie C. Wahlgren. "Protein—Surfactant Interactions at Solid Surfaces." In ACS Symposium Series, 239–54. Washington, DC: American Chemical Society, 1995. http://dx.doi.org/10.1021/bk-1995-0602.ch017.

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Narváez, Alfredo R., and Shyam V. Vaidya. "Protein—Surfactant Interactions at the Air-Water Interface." In Excipient Applications in Formulation Design and Drug Delivery, 139–66. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-20206-8_6.

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Thakur, Gargi, Lakshna Mahajan, Anuvinder Kaur, Roberta Bulla, Uday Kishore, and Taruna Madan. "Surfactant Protein D in Immune Surveillance Against Cancer." In The Collectin Protein Family and Its Multiple Biological Activities, 147–63. Cham: Springer International Publishing, 2021. http://dx.doi.org/10.1007/978-3-030-67048-1_7.

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Panos, Ralph J., and James P. Bridges. "Mutations in Surfactant Protein C and Interstitial Lung Disease." In Molecular Basis of Pulmonary Disease, 133–66. Totowa, NJ: Humana Press, 2010. http://dx.doi.org/10.1007/978-1-59745-384-4_6.

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Brouwer, Wilfried M. "Surfactant and Protein Adsorption at Surface Modified Polystyrene Latices." In Integration of Fundamental Polymer Science and Technology—4, 159–63. Dordrecht: Springer Netherlands, 1990. http://dx.doi.org/10.1007/978-94-009-0767-6_20.

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Sun, Shuo, Caleb I. Neufeld, Ramil F. Latypov, Bernardo Perez-Ramirez, and Qiaobing Xu. "Biophysical Methods for the Studies of Protein-Lipid/Surfactant Interactions." In ACS Symposium Series, 355–75. Washington, DC: American Chemical Society, 2015. http://dx.doi.org/10.1021/bk-2015-1215.ch017.

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Singh, Iesha, Nazar Beirag, Uday Kishore, and Mohamed H. Shamji. "Surfactant Protein D: A Therapeutic Target for Allergic Airway Diseases." In The Collectin Protein Family and Its Multiple Biological Activities, 135–45. Cham: Springer International Publishing, 2021. http://dx.doi.org/10.1007/978-3-030-67048-1_6.

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Conference papers on the topic "Protein-Surfactant"

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Douda, David N., Hartmut Grasemann, and Nades Palaniyar. "Surfactant Protein D Regulates NETosis." In American Thoracic Society 2012 International Conference, May 18-23, 2012 • San Francisco, California. American Thoracic Society, 2012. http://dx.doi.org/10.1164/ajrccm-conference.2012.185.1_meetingabstracts.a3283.

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Chodankar, S. N., V. K. Aswal, A. G. Wagh, Abarrul Ikram, Agus Purwanto, Sutiarso, Anne Zulfia, Sunit Hendrana, and Zeily Nurachman. "Structural Studies of Protein-Surfactant Complexes." In NEUTRON AND X-RAY SCATTERING 2007: The International Conference. AIP, 2008. http://dx.doi.org/10.1063/1.2906038.

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Ikegami, M., SN Grant, TR Korfhagen, and JA Whitsett. "Surfactant Protein-D Controls Surfactant Lipid Content during Postnatal Lung Development." In American Thoracic Society 2009 International Conference, May 15-20, 2009 • San Diego, California. American Thoracic Society, 2009. http://dx.doi.org/10.1164/ajrccm-conference.2009.179.1_meetingabstracts.a2644.

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Mehan, Sumit, V. K. Aswal, and J. Kohlbrecher. "Probing nanoparticle effect in protein-surfactant complexes." In NANOFORUM 2014. AIP Publishing LLC, 2015. http://dx.doi.org/10.1063/1.4917667.

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XiHuai Qiang and Hongyan Feng. "Preparation of protein-surfactant with waste feather." In 2011 International Conference on Remote Sensing, Environment and Transportation Engineering (RSETE). IEEE, 2011. http://dx.doi.org/10.1109/rsete.2011.5965769.

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Gow, Andrew J., and ChangJiang Guo. "Surfactant Protein-D Regulates Alveolar Macrophage Phenotype." In American Thoracic Society 2011 International Conference, May 13-18, 2011 • Denver Colorado. American Thoracic Society, 2011. http://dx.doi.org/10.1164/ajrccm-conference.2011.183.1_meetingabstracts.a1085.

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Mulugeta, Surafel, Adam Kotorashvili, Ming Zhao, Wenge Ding, and Michael F. Beers. "Abnormal Trafficking And Processing Of The Surfactant Protein C I73T Mutant Protein." In American Thoracic Society 2010 International Conference, May 14-19, 2010 • New Orleans. American Thoracic Society, 2010. http://dx.doi.org/10.1164/ajrccm-conference.2010.181.1_meetingabstracts.a2446.

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Mehan, Sumit, Vinod K. Aswal, and Joachim Kohlbrecher. "Structural study of surfactant-dependent interaction with protein." In NANOFORUM 2014. AIP Publishing LLC, 2015. http://dx.doi.org/10.1063/1.4917622.

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Saha, Debasish, Debes Ray, Joachim Kohlbrecher, and Vinod K. Aswal. "Random flight model analysis of protein-surfactant complexes." In DAE SOLID STATE PHYSICS SYMPOSIUM 2018. AIP Publishing, 2019. http://dx.doi.org/10.1063/1.5112872.

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Arroyo Rodriguez, Raquel, Meraj A. Khan, Mercedes Echaide, Nades Palaniyar, and Jesús Perez-Gil. "Surfactant protein SP-D to the rescue of NETosis and NET-induced lung surfactant inactivation." In Abstracts from the 17th ERS Lung Science Conference: ‘Mechanisms of Acute Exacerbation of Respiratory Disease’. European Respiratory Society, 2019. http://dx.doi.org/10.1183/23120541.lungscienceconference-2019.pp211.

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Reports on the topic "Protein-Surfactant"

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Boston, Mark E., G. C. Frech, Enrique Chacon-Cruz, E. S. Buescher, and David G. Oelberg. Surfactant Releases Internal Calcium Stores in Neutrophils by G Protein-Mediated Pathway. Fort Belvoir, VA: Defense Technical Information Center, October 2002. http://dx.doi.org/10.21236/ada413640.

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2

Sela, Shlomo, and Michael McClelland. Investigation of a new mechanism of desiccation-stress tolerance in Salmonella. United States Department of Agriculture, January 2013. http://dx.doi.org/10.32747/2013.7598155.bard.

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Abstract:
Low-moisture foods (LMF) are increasingly involved in foodborne illness. While bacteria cannot grow in LMF due to the low water content, pathogens such as Salmonella can still survive in dry foods and pose health risks to consumer. We recently found that Salmonella secretes a proteinaceous compound during desiccation, which we identified as OsmY, an osmotic stress response protein of 177 amino acids. To elucidate the role of OsmY in conferring tolerance against desiccation and other stresses in Salmonella entericaserovarTyphimurium (STm), our specific objectives were: (1) Characterize the involvement of OsmY in desiccation tolerance; (2) Perform structure-function analysis of OsmY; (3) Study OsmY expression under various growth- and environmental conditions of relevance to agriculture; (4) Examine the involvement of OsmY in response to other stresses of relevance to agriculture; and (5) Elucidate regulatory pathways involved in controlling osmY expression. We demonstrated that an osmY-mutant strain is impaired in both desiccation tolerance (DT) and in long-term persistence during cold storage (LTP). Genetic complementation and addition of a recombinantOsmY (rOsmY) restored the mutant survival back to that of the wild type (wt). To analyze the function of specific domains we have generated a recombinantOsmY (rOsmY) protein. A dose-response DT study showed that rOsmY has the highest protection at a concentration of 0.5 nM. This effect was protein- specific as a comparable amount of bovine serum albumin, an unrelated protein, had a three-time lower protection level. Further characterization of OsmY revealed that the protein has a surfactant activity and is involved in swarming motility. OsmY was shown to facilitate biofilm formation during dehydration but not during bacterial growth under optimal growth conditions. This finding suggests that expression and secretion of OsmY under stress conditions was potentially associated with facilitating biofilm production. OsmY contains two conserved BON domains. To better understand the role of the BON sites in OsmY-mediated dehydration tolerance, we have generated two additional rOsmY constructs, lacking either BON1 or BON2 sites. BON1-minus (but not BON2) protein has decreased dehydration tolerance compared to intact rOsmY, suggesting that BON1 is required for maximal OsmY-mediated activity. Addition of BON1-peptide at concentration below 0.4 µM did not affect STm survival. Interestingly, a toxic effect of BON1 peptide was observed in concentration as low as 0.4 µM. Higher concentrations resulted in complete abrogation of the rOsmY effect, supporting the notion that BON-mediated interaction is essential for rOsmY activity. We performed extensive analysis of RNA expression of STm undergoing desiccation after exponential and stationary growth, identifying all categories of genes that are differentially expressed during this process. We also performed massively in-parallel screening of all genes in which mutation caused changes in fitness during drying, identifying over 400 such genes, which are now undergoing confirmation. As expected OsmY is one of these genes. In conclusion, this is the first study to identify that OsmY protein secreted during dehydration contributes to desiccation tolerance in Salmonella by facilitating dehydration- mediated biofilm formation. Expression of OsmY also enhances swarming motility, apparently through its surfactant activity. The BON1 domain is required for full OsmY activity, demonstrating a potential intervention to reduce pathogen survival in food processing. Expression and fitness screens have begun to elucidate the processes of desiccation, with the potential to uncover additional specific targets for efforts to mitigate pathogen survival in desiccation.
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