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Host Response and Inflammation

A 20-Mer Peptide Derived from the Lectin Domain of SP-A2 Decreases Tumor Necrosis Factor Alpha Production during Mycoplasma pneumoniae Infection

Usir S. Younis, Hong Wei Chu, Monica Kraft, Julie G. Ledford
Sabine Ehrt, Editor
Usir S. Younis
aDepartment of Medicine, University of Arizona, Tucson, Arizona, USA
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Hong Wei Chu
bNational Jewish Health, Denver, Colorado, USA
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Monica Kraft
aDepartment of Medicine, University of Arizona, Tucson, Arizona, USA
cAsthma and Airway Disease Research Center, Tucson, Arizona, USA
fBIO5, University of Arizona, Tucson, Arizona, USA
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Julie G. Ledford
cAsthma and Airway Disease Research Center, Tucson, Arizona, USA
dDepartment of Immunobiology, University of Arizona, Tucson, Arizona, USA
eDepartment of Cellular and Molecular Medicine, University of Arizona, Tucson, Arizona, USA
fBIO5, University of Arizona, Tucson, Arizona, USA
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Sabine Ehrt
Weill Cornell Medical College
Roles: Editor
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DOI: 10.1128/IAI.00099-20
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ABSTRACT

Human surfactant protein-A2 (hSP-A2) is a component of pulmonary surfactant that plays an important role in the lung’s immune system by interacting with viruses, bacteria, and fungi to facilitate pathogen clearance and by downregulating inflammatory responses after an allergic challenge. Genetic variation in SP-A2 at position Gln223Lys is present in up to ∼30% of the population and has been associated with several lung diseases, such as asthma, pulmonary fibrosis, and lung cancer (M. M. Pettigrew, J. F. Gent, Y. Zhu, E. W. Triche, et al., BMC Med Genet 8:15, 2007, https://bmcmedgenet.biomedcentral.com/articles/10.1186/1471-2350-8-15; Y. Wang, P. J. Kuan, C. Zing, J. T. Cronkhite, et al., Am J Hum Genet 84:52–59, 2009, https://www.cell.com/ajhg/fulltext/S0002-9297(08)00595-8). Previous work performed by our group showed differences in levels of SP-A binding to non-live mycoplasma membrane fractions that were dependent on the presence of a lysine (K) or a glutamine (Q) at amino acid position 223 in the carbohydrate region of SP-A2. On the basis of these differences, we have derived 20-amino-acid peptides flanking this region of interest in order to test the ability of each to regulate various immune responses to live Mycoplasma pneumoniae in SP-A knockout mice and RAW 264.7 cells. In both models, the 20-mer containing 223Q significantly decreased both tumor necrosis factor alpha (TNF-α) mRNA levels and protein levels in comparison to the 20-mer containing 223K during M. pneumoniae infection. While neither of the 20-mer peptides (223Q and 223K) had an effect on p38 phosphorylation during M. pneumoniae infection, the 223Q-20mer peptide significantly reduced NF-κB p65 phosphorylation in both models. Taken together, our data suggest that small peptides derived from the lectin domain of SP-A2 that contain the major allelic variant (223Q) maintain activity in reducing TNF-α induction during M. pneumoniae infection.

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A 20-Mer Peptide Derived from the Lectin Domain of SP-A2 Decreases Tumor Necrosis Factor Alpha Production during Mycoplasma pneumoniae Infection
Usir S. Younis, Hong Wei Chu, Monica Kraft, Julie G. Ledford
Infection and Immunity Aug 2020, 88 (9) e00099-20; DOI: 10.1128/IAI.00099-20

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A 20-Mer Peptide Derived from the Lectin Domain of SP-A2 Decreases Tumor Necrosis Factor Alpha Production during Mycoplasma pneumoniae Infection
Usir S. Younis, Hong Wei Chu, Monica Kraft, Julie G. Ledford
Infection and Immunity Aug 2020, 88 (9) e00099-20; DOI: 10.1128/IAI.00099-20
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KEYWORDS

Mycoplasma pneumoniae
tumor necrosis factor alpha
SP-A2
NF-κB

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