Evidence map›Paper›PMID 18086812›Full record

ArticleInfection and immunity2008

Physical linkage of naturally complexed bacterial outer membrane proteins enhances immunogenicity.

Henriette Macmillan, Junzo Norimine, Kelly A Brayton, Guy H Palmer, Wendy C Brown

Open access · greenAbstract read
In one paragraph

Article in Infection and immunity, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

14 citing papers in PubMed, 26 citations in OpenAlex.

  1. Immunization withVaccines · 2023
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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

5 authors at 1 institution in 1 country.

Henriette MacmillanDepartment of Veterinary Microbiology and Pathology, Washington State University, Pullman, WA 99164, USA.
Junzo Norimine
Kelly A Brayton
Guy H Palmer
Wendy C Brown
Washington State University · US

Funding

Immunogenicity of the Type IV Secretin SystemR01AI053692 · NIAID · WASHINGTON STATE UNIVERSITY · PI BROWN, WENDY CATHERINE · 2003 to 2012
$3.3M
NIAID NIH HHS AI053692NIAID NIH HHS R01 AI053692
6 · The paper itself

Abstract

The outer membrane proteins (OMPs) of bacterial pathogens are essential for their growth and survival and especially for attachment and invasion of host cells. Since the outer membrane is the interface between the bacterium and the host cell, outer membranes and individual OMPs are targeted for development of vaccines against many bacterial diseases. Whole outer membrane fractions often protect against disease, and this protection cannot be fully reproduced by using individual OMPs. Exactly how the interactions among individual OMPs influence immunity is not well understood. We hypothesized that one OMP rich in T-cell epitopes can act as a carrier for an associated OMP which is poor in T-cell epitopes to generate T-dependent antibody responses, similar to the hapten-carrier effect. Major surface protein 1a (MSP1a) and MSP1b1 occur as naturally complexed OMPs in the Anaplasma marginale outer membrane. Previous studies demonstrated that immunization with the native MSP1 heteromer induced strong immunoglobulin G (IgG) responses to both proteins, but only MSP1a stimulated strong CD4+ T-cell responses. Therefore, to test our hypothesis, constructs of CD4+ T-cell epitopes from MSP1a linked to MSP1b1 were compared with individually administered MSP1a and MSP1b1 for induction of MSP1b-specific IgG. By linking the T-cell epitopes from MSP1a to MSP1b1, significantly higher IgG titers against MSP1b1 were induced. Understanding how the naturally occurring intermolecular interactions between OMPs influence the immune response may lead to more effective vaccine design.

Indexed as

Anaplasma marginaleAnimalsAntibodies, BacterialBacterial Outer Membrane ProteinsCattleCell ProliferationEpitopes, T-LymphocyteImmunoblottingImmunoglobulin GMacromolecular SubstancesRecombinant Fusion ProteinsT-LymphocytesAntibodies, BacterialBacterial Outer Membrane ProteinsEpitopes, T-LymphocyteImmunoglobulin GMacromolecular Substancesmajor surface protein 1a, Anaplasmamajor surface protein 1b, AnaplasmaRecombinant Fusion Proteins

Identifiers

PMID18086812
PMCPMC2258817
OpenAlexW2152850210

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.