FACTORS INFLUENCING THE GROWTH AND STORAGE OF M. GALLISEPTICUM PROPAGATED IN EMBRYONATED CHICKEN EGGS

1967 ◽  
Vol 143 (1 Biology of th) ◽  
pp. 256-267 ◽  
Author(s):  
R. F. Gentry ◽  
C. T. Kantor ◽  
D. Marthouse
2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Marloes Heijne ◽  
Martina Jelocnik ◽  
Alexander Umanets ◽  
Michael S. M. Brouwer ◽  
Annemieke Dinkla ◽  
...  

AbstractChlamydia gallinacea is an obligate intracellular bacterium that has recently been added to the family of Chlamydiaceae. C. gallinacea is genetically diverse, widespread in poultry and a suspected cause of pneumonia in slaughterhouse workers. In poultry, C. gallinacea infections appear asymptomatic, but studies about the pathogenic potential are limited. In this study two novel sequence types of C. gallinacea were isolated from apparently healthy chickens. Both isolates (NL_G47 and NL_F725) were closely related to each other and have at least 99.5% DNA sequence identity to C. gallinacea Type strain 08-1274/3. To gain further insight into the pathogenic potential, infection experiments in embryonated chicken eggs and comparative genomics with Chlamydia psittaci were performed. C. psittaci is a ubiquitous zoonotic pathogen of birds and mammals, and infection in poultry can result in severe systemic illness. In experiments with embryonated chicken eggs, C. gallinacea induced mortality was observed, potentially strain dependent, but lower compared to C. psittaci induced mortality. Comparative analyses confirmed all currently available C. gallinacea genomes possess the hallmark genes coding for known and potential virulence factors as found in C. psittaci albeit to a reduced number of orthologues or paralogs. The presence of potential virulence factors and the observed mortality in embryonated eggs indicates C. gallinacea should rather be considered as an opportunistic pathogen than an innocuous commensal.


1976 ◽  
Vol 4 (1) ◽  
pp. 104-105
Author(s):  
C. L. Kelling ◽  
I. A. Schipper

The simple syringe-stabilizer unit described in this note provides a means for rapid intravascular inoculation of embryonated chicken eggs with minimal embryonic death from vascular trauma.


2021 ◽  
Author(s):  
Frederick Porter

Introduction Vaccines are biological products that elicit a protective immune response. The details of the manufacturing processes are varied depending on the particular characteristics of the vaccine. There are classically, three basic types of vaccines against viral and bacterial pathogens (For mRNA-, DNA- and vector-vaccines see Chapters 7, 8, 9): Live-attenuated. Killed (non-live). Subunit. “Classical” Vaccine Production The basic classical process includes 5 phases: expression, harvest, inactivation, purification, formulation. The expression systems for viral and bacterial vaccines are distinct. Bacterial expression is performed in fermenters. Viral vaccines are produced in animal cell culture or embryonated chicken eggs. Processes for whole viral or bacterial vaccines often involve only limited processing after expression. Subunit vaccines routinely require the most purification to separate the product from other contaminants. Challenges Challenges for bacterial vaccines include testing to ensure the safety and efficacy of the product. Inactivation procedures need to be carefully controlled. Live attenuated vaccines need to be tested to ensure the vaccine strains are still safe and effective. Viral vaccines require testing to ensure foreign infectious agents are not introduced during processing. Both cultured cells and egg present risks for infection. Live viral vaccines and gene vectors need to be carefully engineered and tested to minimize safety concerns. Highly variable vaccine targets such as influenza need to be re-adapted to current circulating strains.


1998 ◽  
Vol 44 (3) ◽  
pp. 571-577 ◽  
Author(s):  
Lynley K Lewis ◽  
Mary W Smith ◽  
Timothy G Yandle ◽  
A Mark Richards ◽  
M Gary Nicholls

Abstract We describe a specific and sensitive RIA for human adrenomedullin (AM)(1–52). The detection limit and the concentration required for 50% inhibition of binding were 0.1 and 1.2 fmol/tube, respectively. Cross-reactivities with AM(1–12), AM(13–52), calcitonin gene-related peptide, amylin, and other vasoactive hormones were negligible. AM immunoreactivity in normal subjects ranged from 2.7 to 10.1 pmol/L (n = 44). We investigated factors influencing the recovery and measurement of AM in the assay. Recovery of labeled AM (>80%) was markedly higher than that of unlabeled AM (56%). Immunoreactivity of exogenous AM added to plasma decreased up to 70% over four freeze–thaw cycles, whereas endogenous AM was stable. Alkali-treated casein (1 g/L) reduced adsorption of AM to surfaces and significantly increased assay precision compared with bovine serum albumin (P <0.0001). HPLC separation of extracted plasma verified the presence of AM(1–52). We suggest that considerable care is needed to ensure that accurate and reproducible results are obtained from studies quantifying this peptide.


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