Association of Mannose‐Binding Lectin Deficiency with Acute Invasive Aspergillosis in Immunocompromised Patients

Lambourne, Jonathan; Agranoff, Dan; Herbrecht, Raoul; Troke, Peter F.; Buchbinder, Aby; Willis, Fenella; Letscher-Bru, Valérie; Agrawal, Samir; Doffman, Sarah; Johnson, Elizabeth; White, P. Lewis; Barnes, Rosemary Ann; Griffin, George E.; Lindsay, Jodi A.; Harrison, Thomas S.

doi:10.1086/644619

Cited by 82 publications

(64 citation statements)

References 46 publications

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“…By using this approach and using Mascot search, three main protein hits were identified with sequence ID of G3MZ19, F1N1Z8, and F1MCV8 ( Additionally, from the UniProt 12_11, it was mentioned that the sequence ID G3MZ19 is a member of the mannose-binding protein or mannose-binding lectin (MBL) family. Mannose-binding lectin is known to give an important contribution to innate immune defense (van Asbeck et al, 2008;Lambourne et al, 2009). Although less information is available regarding MBL and its role in the saliva of cattle, especially the Bali breed, the presence of MBL-like family in the saliva of Bali cattle possibly contributes to the innate immunity that works together with epithelial barriers around the oral cavity as the first line protection system against pathogens.…”

Section: Resultsmentioning

confidence: 99%

Proteomic Analysis of a 14.2 kDa Protein Isolated from Bali Cattle(Bos Sondaicus/Javanicus)Saliva Using Single Dimension Sodium Dodecyl Sulphate-Polyacrylamide Gel Electrophoresis and Matrix-Assisted Laser Desorption Ionization Time-of-Flight Tandem Mass Spectrometer

Depamede

2013

Italian Journal of Animal Science

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A 14.2 kDa protein isolated from Bali cattle (Bos sondaicus/javanicus) saliva has been reported to have a bactericidal activity. The aim of this study was to analyse the nature of a 14.2 kDa protein using single dimension (1-D) sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and matrix-assisted laser desorption ionization time-of-flight tandem mass spectrometer (MALDI TOF/TOF). The protein was isolated by means of polyethylene glycol (PEG)/sodium sulfate aqueous twophase system, and then determined by 12.5% SDS-PAGE. A band of 14.2 kDa was sliced and analysed by MALDI TOF/TOF mass spectrometer using a 5800 proteomics analyzer. Mascot search and National Center for Biotechnology Information (NCBI) Blast search revealed that the spot of 1-D SDS-PAGE consisted of three proteins: zymogen granule protein 16 homologue B, pancreatic adenocarcinoma upregulated factor-like, and prolactin-inducible protein homologue precursor. The three proteins have been observed in Bos taurus and other species such as mouse. The actual nature of the proteins and their function in Bali cattle (Bos sondaicus/javanicus), as well as the connection with the evolution of bovines need further analysis.

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Section: Resultsmentioning

confidence: 99%

Proteomic Analysis of a 14.2 kDa Protein Isolated from Bali Cattle(Bos Sondaicus/Javanicus)Saliva Using Single Dimension Sodium Dodecyl Sulphate-Polyacrylamide Gel Electrophoresis and Matrix-Assisted Laser Desorption Ionization Time-of-Flight Tandem Mass Spectrometer

Depamede

2013

Italian Journal of Animal Science

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“…Patients with invasive aspergillosis had lower mean MBL levels (281 ng/ml) than patients without aspergillosis (835 ng/ml). MBL deficiency, defined in that study as a level of Ͻ500 ng/ml, was seen more commonly in persons with invasive aspergillosis than in the control population (62% versus 32%) (243). A small study has cited an association between low MBL levels and chronic necrotizing pulmonary aspergillosis (CNPA) (also known as "semi-invasive aspergillosis").…”

Section: Inherited Deficiencies Of Complement Activationmentioning

confidence: 96%

Infections of People with Complement Deficiencies and Patients Who Have Undergone Splenectomy

2010

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SUMMARY The complement system comprises several fluid-phase and membrane-associated proteins. Under physiological conditions, activation of the fluid-phase components of complement is maintained under tight control and complement activation occurs primarily on surfaces recognized as “nonself” in an attempt to minimize damage to bystander host cells. Membrane complement components act to limit complement activation on host cells or to facilitate uptake of antigens or microbes “tagged” with complement fragments. While this review focuses on the role of complement in infectious diseases, work over the past couple of decades has defined several important functions of complement distinct from that of combating infections. Activation of complement in the fluid phase can occur through the classical, lectin, or alternative pathway. Deficiencies of components of the classical pathway lead to the development of autoimmune disorders and predispose individuals to recurrent respiratory infections and infections caused by encapsulated organisms, including Streptococcus pneumoniae, Neisseria meningitidis, and Haemophilus influenzae. While no individual with complete mannan-binding lectin (MBL) deficiency has been identified, low MBL levels have been linked to predisposition to, or severity of, several diseases. It appears that MBL may play an important role in children, who have a relatively immature adaptive immune response. C3 is the point at which all complement pathways converge, and complete deficiency of C3 invariably leads to severe infections, including those caused by meningococci and pneumococci. Deficiencies of the alternative and terminal complement pathways result in an almost exclusive predisposition to invasive meningococcal disease. The spleen plays an important role in antigen processing and the production of antibodies. Splenic macrophages are critical in clearing opsonized encapsulated bacteria (such as pneumococci, meningococci, and Escherichia coli) and intraerythrocytic parasites such as those causing malaria and babesiosis, which explains the fulminant nature of these infections in persons with anatomic or functional asplenia. Paramount to the management of patients with complement deficiencies and asplenia is educating patients about their predisposition to infection and the importance of preventive immunizations and seeking prompt medical attention.

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“…MBL genotype mutations (single nucleotide polymorphisms [SNPs]) have been associated with increased susceptibility to invasive pulmonary aspergillosis (IPA) in humans and types of chronic pulmonary aspergillosis [3,4,[23][24][25][26]. However, high levels of MBL have been found in allergic bronchopulmonary aspergillosis (ABPA) patients and have been correlated with increased IgE, airway hypersensitivity, and increased levels of Th2 cytokines, all associated with asthma [25].…”

Section: Discussionmentioning

confidence: 99%

Resistance of MBL gene-knockout mice to experimental systemic aspergillosis

et al. 2010

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Association of Mannose‐Binding Lectin Deficiency with Acute Invasive Aspergillosis in Immunocompromised Patients

Cited by 82 publications

References 46 publications

Proteomic Analysis of a 14.2 kDa Protein Isolated from Bali Cattle(Bos Sondaicus/Javanicus)Saliva Using Single Dimension Sodium Dodecyl Sulphate-Polyacrylamide Gel Electrophoresis and Matrix-Assisted Laser Desorption Ionization Time-of-Flight Tandem Mass Spectrometer

Proteomic Analysis of a 14.2 kDa Protein Isolated from Bali Cattle(Bos Sondaicus/Javanicus)Saliva Using Single Dimension Sodium Dodecyl Sulphate-Polyacrylamide Gel Electrophoresis and Matrix-Assisted Laser Desorption Ionization Time-of-Flight Tandem Mass Spectrometer

Infections of People with Complement Deficiencies and Patients Who Have Undergone Splenectomy

Resistance of MBL gene-knockout mice to experimental systemic aspergillosis

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