Structural determinants of the interaction between the TpsA and TpsB proteins in the Haemophilus influenzae HMW1 two-partner secretion system

Journal of Bacteriology
Susan GrassJoseph W St Geme

Abstract

The two-partner secretion (TPS) pathway in Gram-negative bacteria consists of a TpsA exoprotein and a cognate TpsB outer membrane pore-forming translocator protein. Previous work has demonstrated that the TpsA protein contains an N-terminal TPS domain that plays an important role in targeting the TpsB protein and is required for secretion. The nontypeable Haemophilus influenzae HMW1 and HMW2 adhesins are homologous proteins that are prototype TpsA proteins and are secreted by the HMW1B and HMW2B TpsB proteins. In the present study, we sought to define the structural determinants of HMW1 interaction with HMW1B during the transport process and while anchored to the bacterial surface. Modeling of HMW1B revealed an N-terminal periplasmic region that contains two polypeptide transport-associated (POTRA) domains and a C-terminal membrane-localized region that forms a pore. Biochemical studies demonstrated that HMW1 engages HMW1B via interaction between the HMW1 TPS domain and the HMW1B periplasmic region, specifically, the predicted POTRA1 and POTRA2 domains. Subsequently, HMW1 is shuttled to the HMW1B pore, facilitated by the N-terminal region, the middle region, and the NPNG motif in the HMW1 TPS domain. Additional analysis reveale...Continue Reading

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Citations

Nov 9, 2019·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·Xiaodan MaGuoyu Meng
May 26, 2017·Frontiers in Cellular and Infection Microbiology·Jeremy GuérinFrançoise Jacob-Dubuisson
Nov 28, 2019·Journal of Proteome Research·Danila Elango, Benjamin L Schulz
Apr 27, 2021·Current Opinion in Structural Biology·Jérémy Guérin, Susan K Buchanan

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