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The nontypeable haemophilus influenzae major adhesin hia is a dual-function lectin that binds to human-specific respiratory tract sialic acid glycan receptors

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Τίτλος: The nontypeable haemophilus influenzae major adhesin hia is a dual-function lectin that binds to human-specific respiratory tract sialic acid glycan receptors
Συγγραφείς: Atack, JM, Day, CJ, Poole, J, Brockman, KL, Timms, JRL, Winter, LE, Haselhorst, T, Bakaletz, LO, Barenkamp, SJ, Jennings, MP
Στοιχεία εκδότη: American Society for Microbiology
Έτος έκδοσης: 2020
Συλλογή: Griffith University: Griffith Research Online
Θεματικοί όροι: Medical Microbiology, Biochemistry and Cell Biology, Biomedical and Clinical Sciences, Biological Sciences, Microbiology, COPD, NTHi, adhesin, autotransporter proteins, bacterial pathogen
Περιγραφή: NTHi is a human-adapted pathogen that colonizes the human respiratory tract. Strains of NTHi express multiple adhesins; however, there is a unique, mutually exclusive relationship between the major adhesins Hia and HMW1 and HMW2 (HMW1/2). Approximately 25% of NTHi strains express Hia, a phase-variable autotransporter protein that has a critical role in colonization of the host nasopharynx. The remaining 75% of strains express HMW1/2. Previous work has shown that the HMW1 and HMW2 proteins mediate binding to 2-3- and 2-6-linked sialic acid glycans found in the human respiratory tract. Here, we show that the high-affinity binding domain of Hia, binding domain 1 (BD1), is responsible for binding to α2-6-sialyllactosamine (2-6 SLN) glycans. BD1 is highly specific for glycans that incorporate the form of sialic acid expressed by humans, N-acetylneuraminic acid (Neu5Ac). We further show that Hia has lower-affinity binding activity for 2-3-linked sialic acid and that this binding activity is mediated via a distinct domain. Thus, Hia with its dual binding activities functionally mimics the combined activities of the HMW1 and HMW2 adhesins. In addition, we show that Hia has a role in biofilm formation by strains of NTHi that express the adhesin. Knowledge of the binding affinity of this major NTHi adhesin and putative vaccine candidate will direct and inform development of future vaccines and therapeutic strategies for this important pathogen. ; Full Text
Τύπος εγγράφου: article in journal/newspaper
Γλώσσα: English
Relation: mBio; Atack, JM; Day, CJ; Poole, J; Brockman, KL; Timms, JRL; Winter, LE; Haselhorst, T; Bakaletz, LO; Barenkamp, SJ; Jennings, MP, The nontypeable haemophilus influenzae major adhesin hia is a dual-function lectin that binds to human-specific respiratory tract sialic acid glycan receptors, mBio, 2020, 11 (6), pp. e02714-20; https://hdl.handle.net/10072/400807
DOI: 10.1128/mBio.02714-20
Διαθεσιμότητα: https://hdl.handle.net/10072/400807
https://doi.org/10.1128/mBio.02714-20
Rights: http://creativecommons.org/licenses/by/4.0/ ; © 2020 Atack et al. This is an openaccess article distributed under the terms of the Creative Commons Attribution 4.0 International license. ; open access
Αριθμός Καταχώρησης: edsbas.7FC06D21
Βάση Δεδομένων: BASE
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  Data: The nontypeable haemophilus influenzae major adhesin hia is a dual-function lectin that binds to human-specific respiratory tract sialic acid glycan receptors
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  Data: <searchLink fieldCode="AR" term="%22Atack%2C+JM%22">Atack, JM</searchLink><br /><searchLink fieldCode="AR" term="%22Day%2C+CJ%22">Day, CJ</searchLink><br /><searchLink fieldCode="AR" term="%22Poole%2C+J%22">Poole, J</searchLink><br /><searchLink fieldCode="AR" term="%22Brockman%2C+KL%22">Brockman, KL</searchLink><br /><searchLink fieldCode="AR" term="%22Timms%2C+JRL%22">Timms, JRL</searchLink><br /><searchLink fieldCode="AR" term="%22Winter%2C+LE%22">Winter, LE</searchLink><br /><searchLink fieldCode="AR" term="%22Haselhorst%2C+T%22">Haselhorst, T</searchLink><br /><searchLink fieldCode="AR" term="%22Bakaletz%2C+LO%22">Bakaletz, LO</searchLink><br /><searchLink fieldCode="AR" term="%22Barenkamp%2C+SJ%22">Barenkamp, SJ</searchLink><br /><searchLink fieldCode="AR" term="%22Jennings%2C+MP%22">Jennings, MP</searchLink>
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  Data: American Society for Microbiology
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  Data: 2020
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  Data: Griffith University: Griffith Research Online
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  Data: <searchLink fieldCode="DE" term="%22Medical+Microbiology%22">Medical Microbiology</searchLink><br /><searchLink fieldCode="DE" term="%22Biochemistry+and+Cell+Biology%22">Biochemistry and Cell Biology</searchLink><br /><searchLink fieldCode="DE" term="%22Biomedical+and+Clinical+Sciences%22">Biomedical and Clinical Sciences</searchLink><br /><searchLink fieldCode="DE" term="%22Biological+Sciences%22">Biological Sciences</searchLink><br /><searchLink fieldCode="DE" term="%22Microbiology%22">Microbiology</searchLink><br /><searchLink fieldCode="DE" term="%22COPD%22">COPD</searchLink><br /><searchLink fieldCode="DE" term="%22NTHi%22">NTHi</searchLink><br /><searchLink fieldCode="DE" term="%22adhesin%22">adhesin</searchLink><br /><searchLink fieldCode="DE" term="%22autotransporter+proteins%22">autotransporter proteins</searchLink><br /><searchLink fieldCode="DE" term="%22bacterial+pathogen%22">bacterial pathogen</searchLink>
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  Data: NTHi is a human-adapted pathogen that colonizes the human respiratory tract. Strains of NTHi express multiple adhesins; however, there is a unique, mutually exclusive relationship between the major adhesins Hia and HMW1 and HMW2 (HMW1/2). Approximately 25% of NTHi strains express Hia, a phase-variable autotransporter protein that has a critical role in colonization of the host nasopharynx. The remaining 75% of strains express HMW1/2. Previous work has shown that the HMW1 and HMW2 proteins mediate binding to 2-3- and 2-6-linked sialic acid glycans found in the human respiratory tract. Here, we show that the high-affinity binding domain of Hia, binding domain 1 (BD1), is responsible for binding to α2-6-sialyllactosamine (2-6 SLN) glycans. BD1 is highly specific for glycans that incorporate the form of sialic acid expressed by humans, N-acetylneuraminic acid (Neu5Ac). We further show that Hia has lower-affinity binding activity for 2-3-linked sialic acid and that this binding activity is mediated via a distinct domain. Thus, Hia with its dual binding activities functionally mimics the combined activities of the HMW1 and HMW2 adhesins. In addition, we show that Hia has a role in biofilm formation by strains of NTHi that express the adhesin. Knowledge of the binding affinity of this major NTHi adhesin and putative vaccine candidate will direct and inform development of future vaccines and therapeutic strategies for this important pathogen. ; Full Text
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  Data: mBio; Atack, JM; Day, CJ; Poole, J; Brockman, KL; Timms, JRL; Winter, LE; Haselhorst, T; Bakaletz, LO; Barenkamp, SJ; Jennings, MP, The nontypeable haemophilus influenzae major adhesin hia is a dual-function lectin that binds to human-specific respiratory tract sialic acid glycan receptors, mBio, 2020, 11 (6), pp. e02714-20; https://hdl.handle.net/10072/400807
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  Data: 10.1128/mBio.02714-20
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  Data: https://hdl.handle.net/10072/400807<br />https://doi.org/10.1128/mBio.02714-20
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  Data: http://creativecommons.org/licenses/by/4.0/ ; © 2020 Atack et al. This is an openaccess article distributed under the terms of the Creative Commons Attribution 4.0 International license. ; open access
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      – TitleFull: The nontypeable haemophilus influenzae major adhesin hia is a dual-function lectin that binds to human-specific respiratory tract sialic acid glycan receptors
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