scholarly journals Surfactant Protein A Binds to the Fusion Glycoprotein of Respiratory Syncytial Virus and Neutralizes Virion Infectivity

1999 ◽  
Vol 180 (6) ◽  
pp. 2009-2013 ◽  
Author(s):  
Reena Ghildyal ◽  
Carol Hartley ◽  
Annalisa Varrasso ◽  
Jayesh Meanger ◽  
Dennis R. Voelker ◽  
...  
1999 ◽  
Vol 103 (7) ◽  
pp. 1015-1021 ◽  
Author(s):  
Ann Marie LeVine ◽  
Jodie Gwozdz ◽  
James Stark ◽  
Michael Bruno ◽  
Jeffrey Whitsett ◽  
...  

2000 ◽  
Vol 13 (1) ◽  
pp. 125-135 ◽  
Author(s):  
TIMOTHY P. HICKLING ◽  
RAJNEESH MALHOTRA ◽  
HELEN BRIGHT ◽  
WILLIAM MCDOWELL ◽  
EDWARD D. BLAIR ◽  
...  

2004 ◽  
Vol 32 (Supplement) ◽  
pp. A115
Author(s):  
Neal J Thomas ◽  
Susan L DiAngelo ◽  
Joanna Floros ◽  
Douglas F Willson ◽  
Wenlei Liu ◽  
...  

2009 ◽  
Vol 297 (4) ◽  
pp. L559-L567 ◽  
Author(s):  
Shirley R. Bruce ◽  
Constance L. Atkins ◽  
Giuseppe N. Colasurdo ◽  
Joseph L. Alcorn

Infection of neonatal lung by respiratory syncytial virus (RSV) is a common cause of respiratory dysfunction. Lung alveolar type II and bronchiolar epithelial (Clara) cells secrete surfactant protein A (SP-A), a collectin that is an important component of the pulmonary innate immune system. SP-A binds to the virus, targeting the infectious agent for clearance by host defense mechanisms. We have previously shown that while the steady-state level of SP-A mRNA increases approximately threefold after RSV infection, steady-state levels of cellular and secreted SP-A protein decrease 40–60% in human type II cells in primary culture, suggesting a mechanism where the virus alters components of the innate immune response in infected cells. In these studies, we find that changes in SP-A mRNA and protein levels in RSV-infected NCI-H441 cells (a bronchiolar epithelial cell line) recapitulate the results in SP-A expression observed in primary lung cells. While SP-A protein is normally ubiquitinated, there is no change in the level of SP-A protein ubiquitination or proteasome activity during RSV infection, suggesting that the reduced levels of SP-A protein are not due to degradation by activated proteasomes. SP-A mRNA is appropriately processed and exported from the nucleus to the cytoplasm during RSV infection. As evidenced by polysome analysis of SP-A mRNA and pulse-chase analysis of newly synthesized SP-A protein, we find a decrease in translational efficiency that is specific for SP-A mRNA. Therefore, the decrease in SP-A protein levels observed after RSV infection of pulmonary bronchiolar epithelial cells results from a mechanism that affects SP-A mRNA translation efficiency.


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