Abstract
Tissue from 13 autopsy cases with invasive gastrointestinal candidiasis was studied for the binding of the pentraxins, C-reactive protein (CRP), pentraxin 3 (PTX3), and serum amyloid P component (SAP) to fungal surfaces. Invasive candidal infection was demonstrated using a hematoxylin and eosin stain and a Gomori methenamine silver stain (GMS). Immunohistochemistry was performed with CRP and PTX3 monoclonal antibodies and did not demonstrate CRP or PTX3 bound to fungi (0 of 13 cases), although CRP was extensively deposited on human tissue. A polyclonal antibody to SAP showed that SAP was bound to fungi in 12 of 13 cases. Although all three pentraxins have been reported to bind to fungi or bacteria, only SAP was bound to filamentous and yeast forms of Candida in human tissue, as detected by immunohistochemistry. SAP was abundantly present on fungi and may have affected the host innate immune response to the invading fungi.
Highlights
Pentraxins are a family of proteins that play an important and integral role in innate immunity.The best characterized pentraxins are C-reactive protein (CRP), pentraxin 3 (PTX3), and serum amyloidP component (SAP)
CRP and serum amyloid P component (SAP) are made in the liver and circulate in the serum, whereas PTX3 is secreted at the local level by numerous cells in response to inflammation
Slide sections found to be positive for Candida species were stained with Gomori methenamine silver (GMS)
Summary
Pentraxins are a family of proteins that play an important and integral role in innate immunity.The best characterized pentraxins are C-reactive protein (CRP), pentraxin 3 (PTX3), and serum amyloidP component (SAP). CRP and SAP (known as short pentraxins based on the primary structure of their subunit) are made in the liver and circulate in the serum, whereas PTX3 is secreted at the local level by numerous cells in response to inflammation. CRP and SAP share an annular shape possessing identical homopentamers, whereas PTX3 (known as a long pentraxin) has a longer N-terminal protein subunit [1]. These proteins have been likened to ancestral antibodies [2]. They are pattern recognizing proteins believed to be important in identifying harmful microbes and helpful in preparing molecules for removal or neutralizing their effects in the host [2]
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