Results 151 to 160 of about 8,266,744 (203)
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Journal of Invertebrate Pathology, 1983
Abstract The presence of a carbohydrate-specific opsonin, distinguishable from hemolymph agglutinin, was demonstrated in the American lobster, Homarus americanus . Hemolymph opsonin, measured by the enhancement of hemocyte phagocytosis of sheep erythrocytes, was found to be more heat and acid labile than the agglutinin.
Arnold H Greenberg
exaly +3 more sources
Abstract The presence of a carbohydrate-specific opsonin, distinguishable from hemolymph agglutinin, was demonstrated in the American lobster, Homarus americanus . Hemolymph opsonin, measured by the enhancement of hemocyte phagocytosis of sheep erythrocytes, was found to be more heat and acid labile than the agglutinin.
Arnold H Greenberg
exaly +3 more sources
European Journal of Immunology, 1997
AbstractSurfactant protein A (SP‐A) and surfactant protein D (SP‐D) are collectins, and both proteins were shown to interact with influenza A virus and alveolar macrophages. However, it is not known whether SP‐A and SP‐D can serve as opsonins for the phagocytosis of influenza A virus by alveolar macrophages.
Jos A. G. Van Strijp +2 more
exaly +5 more sources
AbstractSurfactant protein A (SP‐A) and surfactant protein D (SP‐D) are collectins, and both proteins were shown to interact with influenza A virus and alveolar macrophages. However, it is not known whether SP‐A and SP‐D can serve as opsonins for the phagocytosis of influenza A virus by alveolar macrophages.
Jos A. G. Van Strijp +2 more
exaly +5 more sources
Fish & Shellfish Immunology, 2015
C1q proteins serve as pattern recognition receptors and involve in the pathogen recognition and complement pathway activation. In the present study, a novel C1q domain containing protein from Crassostrea gigas (designated CgC1qDC-1) was isolated by liposaccharide-Sepharose 6B affinity chromatography. The coding sequence of CgC1qDC-1 gene was determined
Shuai Jiang +6 more
semanticscholar +3 more sources
C1q proteins serve as pattern recognition receptors and involve in the pathogen recognition and complement pathway activation. In the present study, a novel C1q domain containing protein from Crassostrea gigas (designated CgC1qDC-1) was isolated by liposaccharide-Sepharose 6B affinity chromatography. The coding sequence of CgC1qDC-1 gene was determined
Shuai Jiang +6 more
semanticscholar +3 more sources
Human opsonins induced during meningococcal disease recognize outer membrane proteins PorA and PorB. [PDF]
Infection and Immunity, 1999 ABSTRACT Human opsonins directed against specific meningococcal outer membrane structures in sera obtained during meningococcal disease were quantified with a recently developed antigen-specific, opsonin-dependent phagocytosis and oxidative burst assay. Outer membrane vesicles (OMVs) and PorA (class 1) and PorB (class 3) proteins
Terje E Michaelsen +2 more
exaly +4 more sources
Developmental & Comparative Immunology, 2012
Proteins containing a scavenger receptor cysteine-rich (SRCR) domain (SRCR proteins) play an important role in the innate immune system of various metazoan animals. In the starfish Asterina pectinifera, mesenchyme cells and coelomocytes govern the two distinct innate immune systems of the larvae and adults, respectively.
Ryohei Furukawa, M. Matsumoto, H. Kaneko
semanticscholar +3 more sources
Proteins containing a scavenger receptor cysteine-rich (SRCR) domain (SRCR proteins) play an important role in the innate immune system of various metazoan animals. In the starfish Asterina pectinifera, mesenchyme cells and coelomocytes govern the two distinct innate immune systems of the larvae and adults, respectively.
Ryohei Furukawa, M. Matsumoto, H. Kaneko
semanticscholar +3 more sources
Blood circulation of soft nanomaterials is governed by dynamic remodeling of protein opsonins at nano-biointerface [PDF]
Nature Communications, 2020 AbstractNanomaterials in the blood must mitigate the immune response to have a prolonged vascular residency in vivo. The composition of the protein corona that forms at the nano-biointerface may be directing this, however, the possible correlation of corona composition with blood residency is currently unknown.
Jayachandran N Kizhakkedathu +2 more
exaly +4 more sources
The human mannose-binding protein functions as an opsonin. [PDF]
Journal of Experimental Medicine, 1989 The human mannose-binding protein (MBP) is a multimeric serum protein that is divided into three domains: a cysteine-rich NH2-terminal domain that stabilizes the alpha-helix of the second collagen-like domain, and a third COOH-terminal carbohydrate binding region.
R A Ezekowitz, K Joiner
exaly +3 more sources
International Journal of Pharmaceutics, 2007
Ken-Ichi Ogawara, Toshikiro Kimura
exaly +2 more sources
Ken-Ichi Ogawara, Toshikiro Kimura
exaly +2 more sources