scholarly journals Production, characterization, and antibody specificity of a mouse monoclonal antibody reactive with Cryptococcus neoformans capsular polysaccharide.

1987 ◽  
Vol 55 (3) ◽  
pp. 742-748 ◽  
Author(s):  
F Dromer ◽  
J Salamero ◽  
A Contrepois ◽  
C Carbon ◽  
P Yeni
2003 ◽  
Vol 10 (5) ◽  
pp. 903-909 ◽  
Author(s):  
Suzanne Brandt ◽  
Peter Thorkildson ◽  
Thomas R. Kozel

ABSTRACT Cryptococcus neoformans is surrounded by an antiphagocytic capsule whose primary constituent is glucuronoxylomannan (GXM). An epitope shared by GXM serotypes A, B, C, and D is immunodominant when mice are immunized with serotype A GXM. In contrast, an epitope shared only by serotypes A and D is immunodominant when mice are immunized with serotype D. Hybridomas secreting antibodies reactive with subdominant epitopes were identified through a positive-negative screening procedure in which antibody-secreting colonies were characterized by reactivity with both the immunizing polysaccharide and GXMs from each of the four major serotypes. In this manner, a monoclonal antibody (MAb) that was reactive with an epitope shared only by serotypes A and B was identified and designated F10F5. Such an epitope has not been described previously. Immunization of mice with de-O-acetylated serotype A GXM generated a hybridoma that secreted an antibody, designated F12D2, that was reactive with all four serotypes. Unlike previously described monoclonal and polyclonal panspecific antibodies, the reactivity of MAb F12D2 was not altered by de-O-acetylation of GXM. These results indicate that there are at least two panspecific GXM epitopes; one epitope is dependent on O acetylation for antibody reactivity, and the other is independent of O acetylation. This study identifies strategies for production of MAbs that are reactive with subdominant or cryptic GXM epitopes and provides new information regarding the antigenic makeup and the humoral immune response to GXM, an essential virulence factor that is a target for active and passive immunization.


2004 ◽  
Vol 72 (6) ◽  
pp. 3674-3679 ◽  
Author(s):  
Luis R. Martinez ◽  
Dariush Moussai ◽  
Arturo Casadevall

ABSTRACT Cryptococcus neoformans releases capsular polysaccharide in the supernatant of liquid cultures and in tissues. Significantly less glucuronoxylomannan (GXM) was released by C. neoformans in the presence of capsule-binding monoclonal antibody (MAb). MAb-mediated inhibition of GXM release may be another mechanism by which humoral immunity can mediate protection against this pathogen.


2009 ◽  
Vol 75 (8) ◽  
pp. 2528-2533 ◽  
Author(s):  
Emma J. Robertson ◽  
Arturo Casadevall

ABSTRACT Most microbes, including the fungal pathogen Cryptococcus neoformans, can grow as biofilms. Biofilms confer upon microbes a range of characteristics, including an ability to colonize materials such as shunts and catheters and increased resistance to antibiotics. Here, we provide evidence that coating surfaces with a monoclonal antibody to glucuronoxylomannan, the major component of the fungal capsular polysaccharide, immobilizes cryptococcal cells to a surface support and, subsequently, promotes biofilm formation. We used time-lapse microscopy to visualize the growth of cryptococcal biofilms, generating the first movies of fungal biofilm growth. We show that when fungal cells are immobilized using surface-attached specific antibody to the capsule, the initial stages of biofilm formation are significantly faster than those on surfaces with no antibody coating or surfaces coated with unspecific monoclonal antibody. Time-lapse microscopy revealed that biofilm growth was a dynamic process in which cells shuffled position during budding and was accompanied by emergence of planktonic variant cells that left the attached biofilm community. The planktonic variant cells exhibited mobility, presumably by Brownian motion. Our results indicate that microbial immobilization by antibody capture hastens biofilm formation and suggest that antibody coating of medical devices with immunoglobulins must exclude binding to common pathogenic microbes and the possibility that this effect could be exploited in industrial microbiology.


Nephron ◽  
1987 ◽  
Vol 46 (1) ◽  
pp. 5-11 ◽  
Author(s):  
Gideon Goldstein

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