Wolbachia surface protein (WSP) inhibits apoptosis in human neutrophils

2007 ◽  
Vol 29 (2) ◽  
Author(s):  
C. BAZZOCCHI ◽  
S. COMAZZI ◽  
R. SANTONI ◽  
C. BANDI ◽  
C. GENCHI ◽  
...  
2000 ◽  
Vol 68 (12) ◽  
pp. 6697-6703 ◽  
Author(s):  
Jason Mott ◽  
Yasuko Rikihisa

ABSTRACT The human granulocytic ehrlichiosis (HGE) agent, which replicates in neutrophils, was found not to induce superoxide anion (O2 −) generation or extracellular release by human peripheral blood neutrophils, as measured by a luminol-dependent chemiluminescence assay or a cytochrome c reduction assay, respectively. Furthermore, the HGE agent completely prevented O2 − release by neutrophils upon stimulation with phorbol myristate acetate (PMA), formylmethionyl-leucyl-phenylalanine, or Escherichia coli. The inhibition was HGE agent dose dependent, required ehrlichial contact with the host cells, and was reversible upon removal of the extracellular HGE agent bound to the host cells prior to PMA stimulation. Structural integrity of or new protein synthesis by the HGE agent was not required for the inhibition; carbohydrate but not surface protein of the HGE agent was required. The HGE agent did not prevent O2 − generation in human peripheral blood monocytes derived from the same individual. This neutrophil-specific prevention of O2 −generation by the HGE agent would be critical in survival of the HGE agent. This is the first demonstration of the rapid inhibition of preexisting NADPH oxidase in human neutrophils by the HGE agent.


2009 ◽  
Vol 77 (12) ◽  
pp. 5659-5667 ◽  
Author(s):  
Maria Lazarou ◽  
José A. Guevara Patiño ◽  
Richard M. Jennings ◽  
Richard S. McIntosh ◽  
Jianguo Shi ◽  
...  

ABSTRACT Antigen-specific antibodies (Abs) to the 19-kDa carboxy-terminal region of Plasmodium falciparum merozoite surface protein 1 (MSP119) play an important role in protective immunity to malaria. Mouse monoclonal Abs (MAbs) 12.10 and 12.8 recognizing MSP119 can inhibit red cell invasion by interfering with MSP1 processing on the merozoite surface. We show here that this ability is dependent on the intact Ab since Fab and F(ab′)2 fragments derived from MAb 12.10, although capable of binding MSP1 with high affinity and competing with the intact antibody for binding to MSP1, were unable to inhibit erythrocyte invasion or MSP1 processing. The DNA sequences of the variable (V) regions of both MAbs 12.8 and 12.10 were obtained, and partial amino acid sequences of the same regions were confirmed by mass spectrometry. Human chimeric Abs constructed by using these sequences, which combine the original mouse V regions with human γ1 and γ3 constant regions, retain the ability to bind to both parasites and recombinant MSP119, and both chimeric human immunoglobulin G1s (IgG1s) were at least as good at inhibiting erythrocyte invasion as the parental murine MAbs 12.8 and 12.10. Furthermore, the human chimeric Abs of the IgG1 class (but not the corresponding human IgG3), induced significant NADPH-mediated oxidative bursts and degranulation from human neutrophils. These chimeric human Abs will enable investigators to examine the role of human Fcγ receptors in immunity to malaria using a transgenic parasite and mouse model and may prove useful in humans for neutralizing parasites as an adjunct to antimalarial drug therapy.


2012 ◽  
Vol 8 (15) ◽  
pp. 711-715 ◽  
Author(s):  
Jayaramaiah Uday ◽  
Hosagavi Puttegowda Puttaraju

Insects ◽  
2019 ◽  
Vol 10 (6) ◽  
pp. 155 ◽  
Author(s):  
Joseph Gichuhi ◽  
Fathiya M. Khamis ◽  
Johnnie Van den Berg ◽  
Sunday Ekesi ◽  
Jeremy K. Herren

Bactrocera dorsalis (Hendel) is an important pest of fruit-bearing plants in many countries worldwide. In Africa, this pest has spread rapidly and has become widely established since the first invasion report in 2003. Wolbachia is a vertically transmitted endosymbiont that can significantly influence aspects of the biology and, in particular, the reproduction of its host. In this study, we screened B. dorsalis specimens collected from several locations in Africa between 2005 and 2017 for Wolbachia using a PCR-based assay to target the Wolbachia surface protein wsp. Of the 357 individuals tested, 10 were positive for Wolbachia using the wsp assay. We identified four strains of Wolbachia infecting two B. dorsalis mitochondrial haplotypes. We found no strict association between the infecting strain and host haplotype, with one strain being present in two different host haplotypes. All the detected strains belonged to Super Group B Wolbachia and did not match any strains reported previously in B. dorsalis in Asia. These findings indicate that diverse Wolbachia infections are present in invasive populations of B. dorsalis.


Blood ◽  
1987 ◽  
Vol 70 (1) ◽  
pp. 60-68 ◽  
Author(s):  
KM Skubitz ◽  
TK Kinkead

Phagocytosis is a critical host defense mechanism of neutrophils. In this study, membrane protein changes occurring during phagocytosis were studied in human neutrophils using surface radiolabeling before or after phagocytosis of various target particles. Cells were labeled at the cell surface using lactoperoxidase-catalyzed iodination or neuraminidase-galactose oxidase-NaB3H4, galactose oxidase-NaB3H4, or periodate-NaB3H4 techniques. Such studies are complicated by the fact that these techniques identify many surface proteins on the phagocyte, and labeling after phagocytosis occurs often results in radiolabeling proteins of the target particle, thus making changes in cell-surface proteins more difficult to detect. Immunoprecipitation with monoclonal antibody AHN-1, which reacts with a carbohydrate present on several human neutrophil surface proteins and inhibits phagocytosis, eliminated interference caused by radiolabeled proteins of the target particle and simplified analysis by restricting the study to a limited number of proteins. AHN-1 immunoprecipitated less radiolabeled protein from neutrophils labeled after phagocytosis of particles opsonized with IgG or complement than from cells labeled before phagocytosis. Isolation of phagocytic vesicles containing opsonized emulsified paraffin oil demonstrated that three proteins of mol wt 105,000, 140,000, and 170,000 recognized by AHN-1 were internalized in the phagocytic vesicle during phagocytosis.


2012 ◽  
Vol 12 (Suppl 1) ◽  
pp. S11 ◽  
Author(s):  
Sofia B Pinto ◽  
Mara Mariconti ◽  
Chiara Bazzocchi ◽  
Claudio Bandi ◽  
Steven P Sinkins

Blood ◽  
1987 ◽  
Vol 70 (1) ◽  
pp. 60-68
Author(s):  
KM Skubitz ◽  
TK Kinkead

Abstract Phagocytosis is a critical host defense mechanism of neutrophils. In this study, membrane protein changes occurring during phagocytosis were studied in human neutrophils using surface radiolabeling before or after phagocytosis of various target particles. Cells were labeled at the cell surface using lactoperoxidase-catalyzed iodination or neuraminidase-galactose oxidase-NaB3H4, galactose oxidase-NaB3H4, or periodate-NaB3H4 techniques. Such studies are complicated by the fact that these techniques identify many surface proteins on the phagocyte, and labeling after phagocytosis occurs often results in radiolabeling proteins of the target particle, thus making changes in cell-surface proteins more difficult to detect. Immunoprecipitation with monoclonal antibody AHN-1, which reacts with a carbohydrate present on several human neutrophil surface proteins and inhibits phagocytosis, eliminated interference caused by radiolabeled proteins of the target particle and simplified analysis by restricting the study to a limited number of proteins. AHN-1 immunoprecipitated less radiolabeled protein from neutrophils labeled after phagocytosis of particles opsonized with IgG or complement than from cells labeled before phagocytosis. Isolation of phagocytic vesicles containing opsonized emulsified paraffin oil demonstrated that three proteins of mol wt 105,000, 140,000, and 170,000 recognized by AHN-1 were internalized in the phagocytic vesicle during phagocytosis.


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