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Vaccine potential of bacterial macrophage infectivity potentiator (MIP)-like peptidyl prolyl cis/trans isomerase (PPIase) proteins

Vaccine potential of bacterial macrophage infectivity potentiator (MIP)-like peptidyl prolyl cis/trans isomerase (PPIase) proteins
Vaccine potential of bacterial macrophage infectivity potentiator (MIP)-like peptidyl prolyl cis/trans isomerase (PPIase) proteins

Peptidyl prolyl cis/trans isomerases (PPIases) are a superfamily of proteins ubiquitously distributed among living organisms, which function primarily to assist the folding and structuring of unfolded and partially folded polypeptide chains and proteins. In this review, we focus specifically on the Macrophage Infectivity Potentiator (MIP)-like PPIases, which are members of the immunophilin family of FK506-binding proteins (FKBP). MIP-like PPIases have accessory roles in virulence and are candidates for inclusion in vaccines protective against both animal and human bacterial pathogens. A structural vaccinology approach obviates any issues over molecular mimicry and potential cross-reactivity with human FKBP proteins and studies with a representative antigen, the Neisseria meningitidis-MIP, support this strategy. Moreover, a dual approach of vaccination and drug targeting could be considered for controlling bacterial infectious diseases of humans and animals.

Amino Acid Sequence, Animals, Bacterial Infections, Bacterial Proteins, Bacterial Vaccines, Drug Design, Humans, Legionella pneumophila, Macrophages, Meningitis, Meningococcal, Molecular Sequence Data, Neisseria meningitidis, Peptidylprolyl Isomerase, Tacrolimus Binding Proteins, Vaccines, Subunit, Journal Article, Research Support, Non-U.S. Gov't, Review
1476-0584
1633-49
Humbert, María Victoria
82134d25-24b8-4fdd-bd1c-461683b5322e
Almonacid Mendoza, Hannia L.
73d16de0-40ef-4ed5-a155-b9b0023c3e82
Jackson, Alexandra C.
eb2e2dd5-0d2c-47af-89a9-09b82f4b4ccb
Hung, Miao-Chiu
38af1a3a-393e-4fd6-a97b-2d2a277319c6
Bielecka, Magdalena K.
90391ea3-aa1f-4104-a893-568c138718a2
Heckels, John E.
fcfcfafe-5ca8-4728-9c5e-cb67f9af7e31
Christodoulides, Myron
eba99148-620c-452a-a334-c1a52ba94078
Humbert, María Victoria
82134d25-24b8-4fdd-bd1c-461683b5322e
Almonacid Mendoza, Hannia L.
73d16de0-40ef-4ed5-a155-b9b0023c3e82
Jackson, Alexandra C.
eb2e2dd5-0d2c-47af-89a9-09b82f4b4ccb
Hung, Miao-Chiu
38af1a3a-393e-4fd6-a97b-2d2a277319c6
Bielecka, Magdalena K.
90391ea3-aa1f-4104-a893-568c138718a2
Heckels, John E.
fcfcfafe-5ca8-4728-9c5e-cb67f9af7e31
Christodoulides, Myron
eba99148-620c-452a-a334-c1a52ba94078

Humbert, María Victoria, Almonacid Mendoza, Hannia L., Jackson, Alexandra C., Hung, Miao-Chiu, Bielecka, Magdalena K., Heckels, John E. and Christodoulides, Myron (2015) Vaccine potential of bacterial macrophage infectivity potentiator (MIP)-like peptidyl prolyl cis/trans isomerase (PPIase) proteins. Expert Review of Vaccines, 14 (12), 1633-49. (doi:10.1586/14760584.2015.1095638).

Record type: Review

Abstract

Peptidyl prolyl cis/trans isomerases (PPIases) are a superfamily of proteins ubiquitously distributed among living organisms, which function primarily to assist the folding and structuring of unfolded and partially folded polypeptide chains and proteins. In this review, we focus specifically on the Macrophage Infectivity Potentiator (MIP)-like PPIases, which are members of the immunophilin family of FK506-binding proteins (FKBP). MIP-like PPIases have accessory roles in virulence and are candidates for inclusion in vaccines protective against both animal and human bacterial pathogens. A structural vaccinology approach obviates any issues over molecular mimicry and potential cross-reactivity with human FKBP proteins and studies with a representative antigen, the Neisseria meningitidis-MIP, support this strategy. Moreover, a dual approach of vaccination and drug targeting could be considered for controlling bacterial infectious diseases of humans and animals.

Full text not available from this repository.

More information

Published date: 15 October 2015
Keywords: Amino Acid Sequence, Animals, Bacterial Infections, Bacterial Proteins, Bacterial Vaccines, Drug Design, Humans, Legionella pneumophila, Macrophages, Meningitis, Meningococcal, Molecular Sequence Data, Neisseria meningitidis, Peptidylprolyl Isomerase, Tacrolimus Binding Proteins, Vaccines, Subunit, Journal Article, Research Support, Non-U.S. Gov't, Review
Organisations: Clinical & Experimental Sciences

Identifiers

Local EPrints ID: 408009
URI: https://eprints.soton.ac.uk/id/eprint/408009
ISSN: 1476-0584
PURE UUID: b6c4019e-850b-4784-8e06-9418dbece7f7

Catalogue record

Date deposited: 06 May 2017 01:06
Last modified: 13 Mar 2019 20:03

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