Evidence map›Paper›PMID 19687208›Full record

ArticleInfection and immunity2009

Structural determinants of autoproteolysis of the Haemophilus influenzae Hap autotransporter.

Roma Kenjale, Guoyu Meng, Doran L Fink, Twyla Juehne, Tomoo Ohashi, Harold P Erickson, Gabriel Waksman, Joseph W St Geme

Open access · greenAbstract read
In one paragraph

Article in Infection and immunity, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
2.3field-weighted citation impact, top 13% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

11 citing papers in PubMed, 16 citations in OpenAlex.

  1. ThemBio · 2026
    Article
  2. Article
  3. Review
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  6. Review
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  11. Structure and function of the Haemophilus influenzae autotransporters.Frontiers in cellular and infection microbiology · 2011
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 4 institutions in 2 countries.

Roma KenjaleDepartment of Pediatrics, Duke University, Durham, NC 27710, USA.
Guoyu Meng
Doran L Fink
Twyla Juehne
Tomoo Ohashi
Harold P Erickson
Gabriel Waksman
Joseph W St Geme
Duke University · USWashington University in St. Louis · USInstitute of Structural and Molecular Biology · GBUniversity College London · GB

Funding

EXTRACELLULAR MATRIX AND CELL ATTACHMENT PROTEINSR01CA047056 · NCI · DUKE UNIVERSITY · PI ERICKSON, HAROLD P · 1988 to 2016
$4.7M
DC-INDUCED HIV-SPECIFIC T CELL IMMUNITYR21AI044322 · NIAID · TULANE UNIVERSITY OF LOUISIANA · PI CURIEL, TYLER J. · 2000 to 2001
$504k
NCI NIH HHS R01 CA047056NIAID NIH HHS AI44322Wellcome TrustWellcome Trust 08087
6 · The paper itself

Abstract

Haemophilus influenzae is a gram-negative bacterium that initiates infection by colonizing the upper respiratory tract. The H. influenzae Hap autotransporter protein mediates adherence, invasion, and microcolony formation in assays with respiratory epithelial cells and presumably facilitates colonization. The serine protease activity of Hap is associated with autoproteolytic cleavage and extracellular release of the HapS passenger domain, leaving the Hapbeta C-terminal domain embedded in the outer membrane. Cleavage occurs most efficiently at the LN1036-37 peptide bond and to a lesser extent at three other sites. In this study, we utilized site-directed mutagenesis, homology modeling, and assays with a peptide library to characterize the structural determinants of Hap proteolytic activity and cleavage specificity. In addition, we used homology modeling to predict the S1, S2, and S4 subsite residues of the Hap substrate groove. Our results indicate that the P1 and P2 positions at the Hap cleavage sites are critical for cleavage, with leucine preferred over larger hydrophobic residues or other amino acids in these positions. The substrate groove is formed by L263 and N274 at the S1 subsite, R264 at the S2 subsite, and E265 at the S4 subsite. This information may facilitate design of approaches to block Hap activity and interfere with H. influenzae colonization.

Indexed as

Amino Acid SequenceBacterial Outer Membrane ProteinsBlotting, WesternHaemophilus influenzaeMolecular Sequence DataMutagenesis, Site-DirectedProtein Structure, QuaternarySequence Homology, Amino AcidSerine EndopeptidasesBacterial Outer Membrane ProteinsHap protein, Hemophilus influenzaeSerine Endopeptidases

Identifiers

PMID19687208
PMCPMC2772505
OpenAlexW2167510725

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.