PMID- 8914753
OWN - NLM
STAT- MEDLINE
DCOM- 19970218
LR  - 20210526
IS  - 1071-412X (Print)
IS  - 1098-6588 (Electronic)
IS  - 1071-412X (Linking)
VI  - 3
IP  - 6
DP  - 1996 Nov
TI  - Evidence for the presence of immunoglobulin E antibodies specific to the cell 
      wall phosphomannoproteins of Candida albicans in patients with allergies.
PG  - 645-50
AB  - To determine the major antigenic component of Candida albicans against 
      immunoglobulin E (IgE) antibodies in the sera of patients with allergies who were 
      positive for IgE antibodies to C. albicans crude antigen in a CAP system, 
      phosphomannoproteins (CAMP/A or CAMP/B for serotype A or B strain, respectively) 
      and their acid-stable portions (CAMP-S/A or CAMP-S/B) were isolated from 
      beta-mercaptoethanol (2-ME) extracts of C. albicans cells of serotypes A and B, 
      and IgE antibodies against these components were compared with those against 
      protein complex and enolase (CAE) fractions isolated from C. albicans cells. The 
      dot blot test, which was used to detect IgE antibodies to the C. albicans 
      antigens, showed that IgE antibodies to the 2-ME extract and phosphomannoprotein 
      fractions were present in the sera of 98.0% (2-ME extract), 96.8% (CAMP/A), 93.2% 
      (CAMP-S/A), 97.2% (CAMP/B), and 81.5% (CAMP-S/B) of the patients, whereas IgE 
      antibodies to the protein complex and CAE fractions were found in the sera of 
      73.6 and 48.8% of the patients, respectively. The extent of IgE binding to the 
      2-ME extract and phosphomannoproteins was well correlated with the fluorescence 
      intensities estimated with the CAP system. Furthermore, the results obtained from 
      the inhibition experiment with the CAP system indicated that the binding of IgE 
      antibodies to Candida antigens is strongly inhibited by the phosphomannoprotein 
      fraction and is an indication that the serum of the patients contained IgE 
      antibodies specific to the cell wall phosphomannoproteins of C. albicans. 
      Finally, an initial chemical analysis indicated that the epitopes for IgE 
      antibodies on the phosphomannoproteins is a carbohydrate portion, since the 
      ability of CAMP/A to inhibit the binding of IgE antibodies to the homologous 
      CAMP/A was destroyed after oxidation by sodium periodate but not after digestion 
      with proteinase K.
FAU - Kanbe, T
AU  - Kanbe T
AD  - Laboratory of Medical Mycology, Nagoya University School of Medicine, Japan. 
      tkanbe@tsuru.med.nagoya.u.ac.jp
FAU - Morishita, M
AU  - Morishita M
FAU - Ito, K
AU  - Ito K
FAU - Tomita, K
AU  - Tomita K
FAU - Utsunomiya, K
AU  - Utsunomiya K
FAU - Ishiguro, A
AU  - Ishiguro A
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Clin Diagn Lab Immunol
JT  - Clinical and diagnostic laboratory immunology
JID - 9421292
RN  - 0 (Antibodies, Fungal)
RN  - 0 (Antigens, Fungal)
RN  - 0 (Fungal Proteins)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Phosphoproteins)
RN  - 0 (mannoproteins)
RN  - 37341-29-0 (Immunoglobulin E)
SB  - IM
MH  - Antibodies, Fungal/*blood
MH  - Antigens, Fungal/immunology/isolation & purification
MH  - Candida albicans/*immunology
MH  - Fungal Proteins/*immunology
MH  - Humans
MH  - Hypersensitivity/*immunology
MH  - Immunoglobulin E/*blood
MH  - Membrane Glycoproteins/*immunology
MH  - Phosphoproteins/*immunology
PMC - PMC170425
EDAT- 1996/11/01 00:00
MHDA- 1996/11/01 00:01
PMCR- 1996/11/01
CRDT- 1996/11/01 00:00
PHST- 1996/11/01 00:00 [pubmed]
PHST- 1996/11/01 00:01 [medline]
PHST- 1996/11/01 00:00 [entrez]
PHST- 1996/11/01 00:00 [pmc-release]
AID - 10.1128/cdli.3.6.645-650.1996 [doi]
PST - ppublish
SO  - Clin Diagn Lab Immunol. 1996 Nov;3(6):645-50. doi: 10.1128/cdli.3.6.645-650.1996.