Abstract
Surfactant protein A (SP-A) inhibits hemagglutination (HA) activity and infectivity of influenza A viruses (IAV). As we have showed before in different assays, SP-A2 gene products are more active than SP-A1. Here, we hypothesized that SP-A1 and SP-A2 mammalian CHO-cell-expressed proteins also differentially modulate HA inhibition of IAV. We found that both SP-A1 and SP-A2 equally displayed α(2,3)-linked sialic acids, and had similar activity against a strain (PR-8) that preferentially binds to α(2,3)-linked sialic acids. Based on these findings, we speculate that in human lung SP-A1 and SP-A2 will not be different in their activity against IAV that preferably bind to α(2,3)-linked sialic acids (like avian strains).
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References
Matrosovich M, Klenk HD (2003) Natural and synthetic sialic acid-containing inhibitors of influenza virus receptor binding. Rev Med Virol 13:85–97
Inkster MD, Hinshaw VS, Schulze IT (1993) The hemagglutinins of duck and human H1 influenza viruses differ in sequence conservation and in glycosylation. J Virol 67:7436–7443
van Eijk M, White MR, Batenburg JJ, Vaandrager AB, van Golde LM, Haagsman HP, Hartshorn KL (2004) Interactions of influenza A virus with sialic acids present on porcine surfactant protein D. Am J Respir Cell Mol Biol 30:871–879
Skehel JJ, Stevens DJ, Daniels RS, Douglas AR, Knossow M, Wilson IA, Wiley DC (1984) A carbohydrate side chain on hemagglutinins of Hong Kong influenza viruses inhibits recognition by a monoclonal antibody. Proc Natl Acad Sci USA 81:1779–1783
Caton AJ, Brownlee GG, Yewdell JW, Gerhard W (1982) The antigenic structure of the influenza virus A/PR/8/34 hemagglutinin (H1 subtype). Cell 31:417–427
Hartshorn KL, Crouch EC, White MR, Eggleton P, Tauber AI, Chang D, Sastry K (1994) Evidence for a protective role of pulmonary surfactant protein D (SP-D) against influenza A viruses. J Clin Invest 94:311–319
Benne CA, Kraaijeveld CA, van Strijp JA, Brouwer E, Harmsen M, Verhoef J, van Golde LM, van Iwaarden JF (1995) Interactions of surfactant protein A with influenza A viruses: binding and neutralization. J Infect Dis 171:335–341
LeVine AM, Hartshorn K, Elliott J, Whitsett J, Korfhagen T (2002) Absence of SP-A modulates innate and adaptive defense responses to pulmonary influenza infection. Am J Physiol Lung Cell Mol Physiol 282:L563–572
Mikerov AN, Umstead TM, Huang W, Liu W, Phelps DS, Floros J (2005) SP-A1 and SP-A2 variants differentially enhance association of Pseudomonas aeruginosa with rat alveolar macrophages. Am J Physiol Lung Cell Mol Physiol 288:L150–L158
Mikerov AN, Wang G, Umstead TM, Zacharatos M, Thomas NJ, Phelps DS, Floros J (2007) SP-A2 variants expressed in CHO-cells stimulate phagocytosis of Pseudomonas aeruginosa more than SP-A1. Infect Immun 75(3):1403–1412
Oberley RE, Snyder JM (2003) Recombinant human SP-A1 and SP-A2 proteins have different carbohydrate-binding characteristics. Am J Physiol Lung Cell Mol Physiol 284:L871–L881
Wang G, Bates-Kenney SR, Tao JQ, Phelps DS, Floros J (2004) Differences in biochemical properties and in biological function between human SP-A1 and SP-A2 variants, and the impact of ozone-induced oxidation. Biochemistry 43:4227–4239
Huang W, Wang G, Phelps DS, Al-Mondhiry H, Floros J (2004) Human SP-A genetic variants and bleomycin-induced cytokine production by THP-1 cells: effect of ozone-induced SP-A oxidation. Am J Physiol Lung Cell Mol Physiol 286:L546–L553
Wang G, Phelps DS, Umstead TM, Floros J (2000) Human SP-A protein variants derived from one or both genes stimulate TNF-alpha production in the THP-1 cell line. Am J Physiol Lung Cell Mol Physiol 278:L946–L954
Wang G, Umstead TM, Phelps DS, Al-Mondhiry H, Floros J (2002) The effect of ozone exposure on the ability of human surfactant protein A variants to stimulate cytokine production. Environ Health Perspect 110:79–84
Garcia-Verdugo I, Wang G, Floros J, Casals C (2002) Structural analysis and lipid-binding properties of recombinant human surfactant protein a derived from one or both genes. Biochemistry 41:14041–14053
Selman M, Lin HM, Montano M, Jenkins AL, Estrada A, Lin Z, Wang G, DiAngelo S, Guo X, Umstead TM, Lang CM, Pardo A, Phelps DS,Floros J (2003) Surfactant protein A and B genetic variants predispose to idiopathic pulmonary fibrosis. Hum Genet 113:542–550
Saitoh H, Okayama H, Shimura S, Fushimi T, Masuda T, Shirato K (1998) Surfactant protein A2 gene expression by human airway submucosal gland cells. Am J Respir Cell Mol Biol 19:202–209
Khubchandani KR, Goss KL, Engelhardt JF, Snyder JM (2001) In situ hybridization of SP-A mRNA in adult human conducting airways. Pediatr Pathol Mol Med 20:349–366
Tagaram HR, Wang G, Umstead TM, Mikerov AN, Thomas NJ, Graff GR, Hess JC, Thomassen MJ, Kavuru MS, Phelps DS, Floros J (2006) Characterization of a human surfactant protein A1 (Sp-A1) gene-specific antibody; Sp-A1 content variation among individuals of varying age and pulmonary health. Am J Physiol Lung Cell Mol Physiol (in press)
Haagsman HP, Hawgood S, Sargeant T, Buckley D, White RT, Drickamer K, Benson BJ (1987) The major lung surfactant protein, SP 28–36, is a calcium-dependent, carbohydrate-binding protein. J Biol Chem 262:13877–13880
Huang W, Wang G, Phelps DS, Al-Mondhiry H, Floros J (2002) Combined SP-A-bleomycin effect on cytokines by THP-1 cells: impact of surfactant lipids on this effect. Am J Physiol Lung Cell Mol Physiol 283:L94–L102
Hartshorn KL, Collamer M, Auerbach M, Myers JB, Pavlotsky N, Tauber AI (1988) Effects of influenza A virus on human neutrophil calcium metabolism. J Immunol 141:1295–1301
Hartshorn KL, White MR, Shepherd V, Reid K, Jensenius JC, Crouch EC (1997) Mechanisms of anti-influenza activity of surfactant proteins A and D: comparison with serum collectins. Am J Physiol 273:L1156–L1166
Kandel R, Hartshorn KL (2005) Novel strategies for prevention and treatment of influenza. Expert Opin Ther Targets 9:1–22
Trampuz A, Prabhu RM, Smith TF, Baddour LM (2004) Avian influenza: a new pandemic threat? Mayo Clin Proc 79:523–530 quiz 530
Webby RJ, Webster RG (2003) Are we ready for pandemic influenza? Science 302:1519–1522
Arnon TI, Achdout H, Lieberman N, Gazit R, Gonen-Gross T, Katz G, Bar-Ilan A, Bloushtain N, Lev M, Joseph A, Kedar E, Porgador A, Mandelboim O (2004) The mechanisms controlling the recognition of tumor- and virus-infected cells by NKp46. Blood 103:664–672
Acknowledgments
This work was supported by the National Institute of Environmental Health Sciences (RO1 ES009882-04A1) and HL69031 (KLH). The authors thank Dr Martin van Eijk for initial pilot experiments with glycan blots, and Karen Chorney for technical assistance.
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Mikerov, A.N., White, M., Hartshorn, K. et al. Inhibition of hemagglutination activity of influenza A viruses by SP-A1 and SP-A2 variants expressed in CHO cells. Med Microbiol Immunol 197, 9–12 (2008). https://doi.org/10.1007/s00430-007-0051-4
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DOI: https://doi.org/10.1007/s00430-007-0051-4