PMID- 7526121
OWN - NLM
STAT- MEDLINE
DCOM- 19941208
LR  - 20240109
IS  - 0950-382X (Print)
IS  - 0950-382X (Linking)
VI  - 10
IP  - 3
DP  - 1993 Nov
TI  - Immunophilins: structure-function relationship and possible role in microbial 
      pathogenicity.
PG  - 445-56
AB  - Immunophilins are housekeeping proteins present in a wide variety of organisms. 
      Members of two protein superfamilies, cyclophilins (Cyps) and FK506-binding 
      proteins (FKBPs) belong to this class of immunophilins. Despite the fact that the 
      amino acid sequences of Cyp and FKBPs do not exhibit noticeable homology to each 
      other, proteins of both classes are able to ligate immunosuppressive peptide 
      derivatives. Cyps form complexes with the cyclic undercapeptide cyclosporin A and 
      FKBPs are able to bind FK506 as well as rapamycin, both of which have a pipecolyl 
      bond within their structure. In a ligand-bound form, immunophilins interfere with 
      signal transduction in T cells. In addition, immunophilins have peptidyl prolyl 
      cis-trans isomerase (PPlase) activity and are able to accelerate the rate of 
      conformational events in proline-containing polypeptides. Microorganisms produce 
      proteins that exhibit extensive sequence homologies to cyclophilins and FKBPs of 
      higher organisms and which have considerable PPlase catalytic activity. While 
      cyclophilins seem to be present in most if not all microbial species 
      investigated, FKBPs are produced by yeasts as well as by a number of pathogenic 
      bacteria, such as Legionella pneumophila, Chlamydia trachomatis and Neisseria 
      meningitidis. The Mip protein of L. pneumophila is a virulence factor that plays 
      an essential role in the ability of the bacteria to survive and multiply in 
      phagocytic cells. Some results are summarized on the structure and putative 
      functions of immunophilins and place special emphasis on the contribution of 
      these polypeptides to the virulence of pathogenic microorganisms.
FAU - Hacker, J
AU  - Hacker J
AD  - Institut fur Molekulare Infektionsbiologie, Wurzburg, Germany.
FAU - Fischer, G
AU  - Fischer G
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Review
PL  - England
TA  - Mol Microbiol
JT  - Molecular microbiology
JID - 8712028
RN  - 0 (Bacterial Proteins)
RN  - 0 (Carrier Proteins)
RN  - 0 (Fungal Proteins)
RN  - 0 (Heat-Shock Proteins)
RN  - 0 (Immunosuppressive Agents)
RN  - 83HN0GTJ6D (Cyclosporine)
RN  - 9DLQ4CIU6V (Proline)
RN  - EC 5.1.1.- (Amino Acid Isomerases)
RN  - EC 5.2.1.- (Tacrolimus Binding Proteins)
RN  - EC 5.2.1.8 (Peptidylprolyl Isomerase)
RN  - WM0HAQ4WNM (Tacrolimus)
SB  - IM
GS  - mip
MH  - Amino Acid Isomerases/chemistry/*physiology
MH  - Amino Acid Sequence
MH  - Bacterial Proteins/chemistry/genetics/physiology
MH  - Carrier Proteins/chemistry/*physiology
MH  - Cyclosporine/metabolism
MH  - Eukaryotic Cells/enzymology
MH  - Fungal Proteins/genetics/physiology
MH  - Heat-Shock Proteins/chemistry/*physiology
MH  - Humans
MH  - Immunosuppressive Agents/*metabolism
MH  - Legionellaceae/enzymology/genetics/pathogenicity
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - Multigene Family
MH  - Peptidylprolyl Isomerase
MH  - Prokaryotic Cells/enzymology
MH  - Proline/chemistry
MH  - Protein Binding
MH  - Protein Conformation
MH  - Sequence Alignment
MH  - Sequence Homology, Amino Acid
MH  - Structure-Activity Relationship
MH  - Tacrolimus/metabolism
MH  - Tacrolimus Binding Proteins
MH  - Virulence
RF  - 92
EDAT- 1993/11/01 00:00
MHDA- 1993/11/01 00:01
CRDT- 1993/11/01 00:00
PHST- 1993/11/01 00:00 [pubmed]
PHST- 1993/11/01 00:01 [medline]
PHST- 1993/11/01 00:00 [entrez]
AID - 10.1111/j.1365-2958.1993.tb00917.x [doi]
PST - ppublish
SO  - Mol Microbiol. 1993 Nov;10(3):445-56. doi: 10.1111/j.1365-2958.1993.tb00917.x.